A metallocarboxypeptidase that removes C-terminal lysine and arginine from biologically active peptides and proteins thereby regulating their activity. It is a zinc enzyme with no preference shown for lysine over arginine. Pro-carboxypeptidase U in human plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U.
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
A ZINC-containing exopeptidase primarily found in SECRETORY VESICLES of endocrine and neuroendocrine cells. It catalyzes the cleavage of C-terminal ARGININE or LYSINE residues from polypeptides and is active in processing precursors of PEPTIDE HORMONES and other bioactive peptides.
A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. The enzyme catalyzes the preferential cleavage of a C-terminal peptidyl-L-lysine or arginine. It was formerly classified as EC 3.4.2.2 and EC 3.4.12.3.
Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC 3.4.2.1 and EC 3.4.12.2.
A metallocarboxypeptidase that removes C-terminal basic amino acid from peptides and proteins, with preference shown for lysine over arginine. It is a plasma zinc enzyme that inactivates bradykinin and anaphylatoxins.
A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.
A metallocarboxypeptidase that is predominantly expressed as a membrane-bound enzyme. It catalyzes the hydrolysis of an unsubstituted, C-terminal glutamyl residue, typically from PTEROYLPOLYGLUTAMIC ACIDS. It was formerly classified as EC 3.4.19.8.
Catalyzes the hydrolysis of pteroylpolyglutamic acids in gamma linkage to pterolylmonoglutamic acid and free glutamic acid. EC 3.4.19.9.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Enzyme which catalyzes the peptide cross-linking of nascent CELL WALL; PEPTIDOGLYCAN.
A carboxypeptidase that is specific for proteins that contain two ALANINE residues on their C-terminal. Enzymes in this class play an important role in bacterial CELL WALL biosynthesis.
Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion.
The rate dynamics in chemical or physical systems.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Peptides composed of two amino acid units.
A penicillin derivative commonly used in the form of its sodium or potassium salts in the treatment of a variety of infections. It is effective against most gram-positive bacteria and against gram-negative cocci. It has also been used as an experimental convulsant because of its actions on GAMMA-AMINOBUTYRIC ACID mediated synaptic transmission.
Physiologically inactive substances that can be converted to active enzymes.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A subclass of lipid-linked proteins that contain a GLYCOSYLPHOSPHATIDYLINOSITOL LINKAGE which holds them to the CELL MEMBRANE.
Serum peptides derived from certain cleaved COMPLEMENT PROTEINS during COMPLEMENT ACTIVATION. They induce smooth MUSCLE CONTRACTION; mast cell HISTAMINE RELEASE; PLATELET AGGREGATION; and act as mediators of the local inflammatory process. The order of anaphylatoxin activity from the strongest to the weakest is C5a, C3a, C4a, and C5a des-arginine.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
The process of cleaving a chemical compound by the addition of a molecule of water.
A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.
An inhibitor of glutamate decarboxylase. It decreases the GAMMA-AMINOBUTYRIC ACID concentration in the brain, thereby causing convulsions.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
The sum of the weight of all the atoms in a molecule.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
A family of neutral serine proteases with CHYMOTRYPSIN-like activity. Chymases are primarily found in the SECRETORY GRANULES of MAST CELLS and are released during mast cell degranulation.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
An imperfect fungus present on most agricultural seeds and often responsible for the spoilage of seeds in bulk storage. It is also used in the production of fermented food or drink, especially in Japan.
A nuclear RNA-protein complex that plays a role in RNA processing. In the nucleoplasm, the U1 snRNP along with other small nuclear ribonucleoproteins (U2, U4-U6, and U5) assemble into SPLICEOSOMES that remove introns from pre-mRNA by splicing. The U1 snRNA forms base pairs with conserved sequence motifs at the 5'-splice site and recognizes both the 5'- and 3'-splice sites and may have a fundamental role in aligning the two sites for the splicing reaction.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, -Xaa-*-Xbb-Xcc, when neither Xaa nor Xbb is Pro. It is a Cl(-)-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. It may also have endopeptidase activity on some substrates. (From Enzyme Nomenclature, 1992) EC 3.4.15.1.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
A family of gram-positive, saprophytic bacteria occurring in soil and aquatic environments.
A genus of gram-positive bacteria in the family Thermoactinomycetaceae, that can cause FARMER'S LUNG.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
A genus of gram-positive bacteria that forms a branched mycelium. It commonly occurs as a saprophytic form in soil and aquatic environments.

Assay of procarboxypeptidase U, a novel determinant of the fibrinolytic cascade, in human plasma. (1/124)

BACKGROUND: Procarboxypeptidase U (proCPU) is a novel proenzyme found in human plasma. The active form, carboxypeptidase U (CPU; EC 3.4.17.20), retards the rate of fibrinolysis through its ability to cleave C-terminal lysine residues on fibrin partially degraded by plasmin. This reduces the number of high-affinity plasminogen-binding sites on fibrin. METHODS: We developed an assay to determine the proCPU concentration in human plasma. The assay involved quantitative conversion of proCPU to active CPU by thrombin-thrombomodulin, a very efficient activator of proCPU, followed by determination of the enzymatic activity of CPU with the substrate hippuryl-L-arginine, using an HPLC-assisted determination of the released hippuric acid. Using this method, we established a reference interval based on 490 healthy individuals. RESULTS: The mean proCPU concentration, determined after activation of the zymogen in diluted plasma and expressed as CPU activity, was 964 U/L, with a SD of 155 U/L. The population showed a gaussian distribution. However, we noticed important differences related to age and the use of hormone preparations. CONCLUSIONS: The sensitivity and precision of the method make it suitable for routine clinical determinations and as a reference procedure.  (+info)

Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains. (2/124)

A collection of 56 purified thrombin mutants, in which 76 charged or polar surface residues on thrombin were mutated to alanine, was used to identify key residues mediating the interactions of thrombin with thrombomodulin (TM), protein C, and thrombin-activatable fibrinolysis inhibitor (TAFI). Comparison of protein C activation in the presence and absence of TM identified 11 residues mediating the thrombin-TM interaction (Lys(21), Gln(24), Arg(62), Lys(65), His(66), Arg(68), Thr(69), Tyr(71), Arg(73), Lys(77), Lys(106)). Three mutants (E25A, D51A, R89A/R93A/E94A) were found to have decreased ability to activate TAFI yet retained normal protein C activation, whereas three other mutants (R178A/R180A/D183A, E229A, R233A) had decreased ability to activate protein C but maintained normal TAFI activation. One mutant (W50A) displayed decreased activation of both substrates. Mapping of these functional residues on thrombin revealed that the 11 residues mediating the thrombin-TM interaction are all located in exosite I. Residues important in TAFI activation are located above the active-site cleft, whereas residues involved in protein C are located below the active-site cleft. In contrast to the extensive overlap of residues mediating TM binding and fibrinogen clotting, these data show that distinct domains in thrombin mediate its interactions with TM, protein C, and TAFI. These studies demonstrate that selective enzymatic properties of thrombin can be dissociated by site-directed mutagenesis.  (+info)

A novel approach to arterial thrombolysis. (3/124)

Achieving early, complete, and sustained reperfusion after acute myocardial infarction does not occur in approximately 50% of patients, even with the most potent established thrombolytic therapy. Bleeding is observed with increased concentrations of thrombolytics as well as with adjunctive antithrombotic and antiplatelet agents. A novel approach to enhance thrombolytic therapy is to inhibit the activated form of thrombin-activatable fibrinolysis inhibitor (TAFI), which attenuates fibrinolysis in clots formed from human plasma. Identification of TAFI in rabbit plasma facilitated the development of a rabbit arterial thrombolysis model to compare the thrombolytic efficacy of tissue-plasminogen activator (tPA) alone or with an inhibitor, isolated from the potato tuber (PTI), of activated TAFI (TAFIa). Efficacy was assessed by determining the time to patency, the time the vessel remained patent, the maximal blood flow achieved during therapy, the percentage of the original thrombus, which lysed, the percentage change in clot weight, the net clot accreted, and the release of radioactive fibrin degradation products into the circulation. The results indicate that coadministration of PTI and tPA significantly improved tPA-induced thrombolysis without adversely affecting blood pressure, activated partial thromboplastin time, thrombin clotting time, fibrinogen, or alpha-2-antiplasmin concentrations. The data indicate that inhibitors of TAFIa may comprise novel and very effective adjuncts to tPA and improve thrombolytic therapy to achieve both clot lysis and vessel patency.  (+info)

Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage. (4/124)

Thrombin-activable fibrinolysis inhibitor (TAFI) is present in the circulation as an inactive zymogen. Thrombin converts TAFI to a carboxypeptidase B-like enzyme (TAFIa) by cleaving at Arg(92) in a process accelerated by the cofactor, thrombomodulin. TAFIa attenuates fibrinolysis. TAFIa can be inactivated by both proteolysis by thrombin and spontaneous temperature-dependent loss of activity. The identity of the thrombin cleavage site responsible for loss of TAFIa activity was suggested to be Arg(330), but site-directed mutagenesis of this residue did not prevent inactivation of TAFIa by thrombin. In this study we followed TAFI activation and TAFIa inactivation by thrombin/thrombomodulin in time and characterized the cleavage pattern of TAFI using matrix-assisted laser desorption ionization mass spectrometry. Mass matching of the fragments revealed that TAFIa was cleaved at Arg(302). Studies of a mutant R302Q-TAFI confirmed identification of this thrombin cleavage site and, furthermore, suggested that inactivation of TAFIa is based on its conformational instability rather than proteolytic cleavage at Arg(302).  (+info)

Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor. (5/124)

We have used site-directed mutagenesis and a recombinant expression system for thrombin-activable fibrinolysis inhibitor (TAFI) in order to identify the thrombin cleavage site in activated TAFI (TAFIa) and to determine the relative contribution of proteolytic cleavage and thermal instability in regulation of TAFIa activity in clots. Arg-330 of TAFIa had been proposed to be the thrombin cleavage site based on studies with trypsin, but mutation of this residue to Gln did not prevent thrombin-mediated cleavage nor did mutation to Gln of the nearby Arg-320 residue. However, mutation of Arg-302 to Gln abolished thrombin-mediated cleavage of TAFIa. All TAFIa variants were susceptible to plasmin cleavage. Interestingly, all Arg to Gln substitutions decreased the thermal stability of TAFIa. The antifibrinolytic potential of the TAFI mutants in vitro correlates with the thermal stability of their respective TAFIa species, indicating that this property plays a key role in regulating the activity if TAFIa. Incubation of TAFIa under conditions that result in complete thermal inactivation of the enzyme accelerates subsequent thrombin- and plasmin-mediated cleavage of TAFIa. Moreover, the extent of cleavage of TAFIa by thrombin does not affect the rate of decay of TAFIa activity. Collectively, these studies point to a role for the thermal instability, but not for proteolytic cleavage, of TAFIa in regulation of its activity and, thus, of its antifibrinolytic potential. Finally, we propose a model for the thermal instability of TAFIa.  (+info)

Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis. (6/124)

Thrombin activatable fibrinolysis inhibitor (TAFI, or procarboxypeptidase B) is the precursor of a recently described carboxypeptidase that potently attenuates fibrinolysis. Therefore, we hypothesized that elevated plasma TAFI levels induce a hypofibrinolytic state associated with an increased risk for venous thrombosis. To evaluate this hypothesis, we developed an electroimmunoassay for TAFI antigen and used this assay to measure TAFI levels in the Leiden Thrombophilia Study, a case-control study of venous thrombosis in 474 patients with a first deep vein thrombosis and 474 age- and sex-matched control subjects. In 474 healthy control subjects, an increase of TAFI with age was observed in women but not in men. Oral contraceptive use also increased the TAFI concentration. TAFI levels above the 90th percentile of the controls (> 122 U/dL) increased the risk for thrombosis nearly 2-fold compared with TAFI levels below the 90th percentile (odds ratio, 1.7; 95% confidence interval, 1.1-2.5). Adjustment for various possible confounders did not materially affect this estimate. These results indicate that elevated TAFI levels form a mild risk factor for venous thrombosis. Such levels were found in 9% of healthy controls and in 14% of patients with a first deep vein thrombosis. Elevated TAFI levels did not enhance the thrombotic risk associated with factor V Leiden but may interact with high factor VIII levels. (Blood. 2000;95:2855-2859)  (+info)

Elements of the primary structure of thrombomodulin required for efficient thrombin-activable fibrinolysis inhibitor activation. (7/124)

Deletion and point mutants of soluble thrombomodulin were used to compare and contrast elements of primary structure required for the activation of thrombin-activable fibrinolysis inhibitor (TAFI) and protein C. The smallest mutant capable of efficiently promoting TAFI activation contained residues including the c-loop of epidermal growth factor-3 (EGF3) through EGF6. This mutant is 13 residues longer than the smallest mutant that functioned well with protein C; the latter consisted of residues from the interdomain loop connecting EGF3 and EGF4 through EGF6. Alanine point mutants showed no loss of function in protein C activation for mutations within the c-loop of EGF3. In TAFI activation, however, alanine mutations cause a 50% reduction at Tyr-337, 67% reductions at Asp-338 and Leu-339, and 90% or greater reductions at Val-340, Asp-341, and Glu-343. A mutation at Asp-349 in the peptide connecting EGF3 to EGF4 eliminated activity against both TAFI and protein C. Oxidation of Met-388 in the peptide connecting EGF5 to EGF6 reduced the rate of protein C activation by 80% but marginally, if at all, affected the rate of TAFI activation. Mutation at Phe-376 severely reduced protein C activation but only marginally influenced that of TAFI. A Q387P mutation, however, severely reduced both activities. TAFI activation was shown to be Ca(2+)-dependent. The response, unlike that of protein C, was monotonic and was half-maximal at 0.25 mm Ca(2+). Like protein C activation, TAFI activation was eliminated by a monoclonal antibody directed at the thrombin-binding domain (EGF5) but was not affected by one directed at EGF2. Thus, elements of structure in the thrombin-binding domain are needed for the activation of both protein C and TAFI, but more of the primary structure is needed for TAFI activation. In addition, some residues are needed for one of the reactions but not the other.  (+info)

Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not. (8/124)

Carboxypeptidase R (EC 3.4.17.20; CPR) and carboxypeptidase N (EC 3. 4.17.3; CPN) cleave carboxyl-terminal arginine and lysine residues from biologically active peptides such as kinins and anaphylatoxins, resulting in regulation of their biological activity. Human proCPR, also known as thrombin-activatable fibrinolysis inhibitor, plasma pro-carboxypeptidase B, and pro-carboxypeptidase U, is a plasma zymogen activated during coagulation. CPN, however, previously termed kininase I and anaphylatoxin inactivator, is present in a stable active form in plasma. We report here the isolation of mouse proCPR and CPN cDNA clones that can induce their respective enzymatic activities in culture supernatants of transiently transfected cells. Potato carboxypeptidase inhibitor can inhibit carboxypeptidase activity in culture medium of mouse proCPR-transfected cells. The expression of proCPR mRNA in murine liver is greatly enhanced following LPS injection, whereas CPN mRNA expression remains unaffected. Furthermore, the CPR activity in plasma increased 2-fold at 24 h after LPS treatment. Therefore, proCPR can be considered a type of acute phase protein, whereas CPN is not. An increase in CPR activity may facilitate rapid inactivation of inflammatory mediators generated at the site of Gram-negative bacterial infection and may consequently prevent septic shock. In view of the ability of proCPR to also inhibit fibrinolysis, an excess of proCPR induced by LPS may contribute to hypofibrinolysis in patients suffering from disseminated intravascular coagulation caused by sepsis.  (+info)

We investigated clot lysis time, thrombin activatable fibrinolysis inhibitor antigen (TAFI) levels and TAFI gene polymorphisms in pregnant patients with severe preeclampsia, with or without associated antiphospholipid syndrome (APS). The study groups
INTRODUCTION: Hypertension is associated with hemostatic abnormalities and endothelial dysfunction. thrombin activatable fibrinolysis inhibitor (TAFI) is a glycoprotein linking coagulation and fibrinolysis. Objectives. We evaluated TAFI concentration
Title: Thrombin-Activatable Fibrinolysis Inhibitor. VOLUME: 11 ISSUE: 17. Author(s):Pauline F. Marx. Affiliation:Dept. Vascular Medicine, G1-114, Academic Medical Center, P.O. Box 22660, 1100 DD Amsterdam, The Netherlands.. Keywords:tafi, cpu, cpr, cpb, carboxypeptidase, coagulation, fibrinolysis. Abstract: The coagulation system is a potent mechanism that prevents blood loss after vascular injury. It consists of a number of linked enzymatic reactions resulting in thrombin generation. Thrombin converts soluble fibrinogen into a fibrin clot. The clot is subsequently removed by the fibrinolytic system upon wound healing. Thrombin-activatable fibrinolysis inhibitor (TAFI), which is identical to the previously identified proteins procarboxypeptidase B, R, and U, forms a link between blood coagulation and fibrinolysis. TAFI circulates as an inactive proenzyme in the bloodstream, and becomes activated during blood clotting. The active form, TAFIa, inhibits fibrinolysis by cleaving off C-terminal ...
Objective: Inflammation and migration of leukocytes to the brain parenchyma play a role in atherosclerosis and cerebral ischemic stroke. Migration occurs with the help of adhesion molecules on the surface of cerebral endothelial cells and leukocytes. P-selectin, an adhesion molecule, is present on the platelet and endothelial surface and allows leukocytes to loosely adhere to the endothelium, and its increase has been shown in acute ischemic stroke (AIS). Thrombin-activatable fibrinolysis inhibitor (TAFI) is a procarboxypeptidase molecule that can be another marker of AIS, which has been shown to increase the risk of thromboembolism and stroke 6-fold. Intima-media thickness (IMT) is thought to be associated with atherosclerotic diseases in carotid ultrasonography (USG) and increased risk of ischemic stroke has been found to be associated with increased carotid IMT. In this study, we investigated the relationship between P-selectin and TAFI levels, which have been shown to be effective for AIS ...
Thrombin-activatable fibrinolysis inhibitor (TAFI) is a metallocarboxypeptidase (MCP) that links blood coagulation and fibrinolysis. TAFI hampers fibrin-clot lysis and is a pharmacological target for the treatment of thrombotic conditions. TAFI is transformed through removal of its prodomain by thrombin-thrombomodulin into TAFIa, which is intrinsically unstable and has a short half-life in vivo. Here we show that purified bovine TAFI activated in the presence of a proteinaceous inhibitor renders a stable enzyme-inhibitor complex. Its crystal structure reveals that TAFIa conforms to the α/β-hydrolase fold of MCPs and displays two unique flexible loops on the molecular surface, accounting for structural instability and susceptibility to proteolysis. In addition, point mutations reported to enhance protein stability in vivo are mainly located in the first loop and in another surface region, which is a potential heparin-binding site. The protein inhibitor contacts both the TAFIa active site and an ...
Carboxypeptidases (CP), carboxypeptidase N (CPN) and carboxypeptidase R (CPR), have been reported as a protease, which can cleave carboxy-terminal arginine or lysine residues from biologically active peptides, such as C3a and C5a, and regulate their activity. CPN is present in the active form in plasma, but CPR is generated from its zymogen during coagulation. CPR (identical to carboxypeptidase U [CPU], plasma carboxypeptidase B [plasma CPB]) has also been described as an inhibitor of fibrinolysis, and termed TAFI (thrombin activatable fibrinolysis inhibitor). ProCPR is activated by thrombin, thrombin-thrombomodulin complex (T-TM), plasmin, and trypsin. Today, the T-TM complex pathway has been taken notice because of effectiveness of Protein C for sepsis. Protein C has been recognized as a mediator between inflammation and coagulation. About CPR, some recent clinical studies have been shown that CPR is an acute phase protein and proCPR have been reduced in DIC. Similar to Protein C, CPR may be a ...
Thrombin activatable fibrinolysis inhibitor (TAFI) is a human plasma-derived zymogen that is activated through proteolytic cleavage by thrombin, thrombin in complex with thrombomodulin, or plasmin. Active TAFI attenuates fibrinolysis by removing carboxyl-terminal lysine residues from partially degraded fibrin, thereby inhibiting a potent positive feedback loop in the fibrinolytic cascade. In addition to the plasma pool of TAFI arising from expression in the liver, a distinct pool of TAFI has been reported to be present in platelets. While the antifibrinolytic effect of plasma-derived TAFI has been well-documented by in vitro and in vivo clot lysis assays, characterization of the platelet-derived form has been limited. Here, we not only confirm the presence of TAFI in the medium of washed, thrombin-stimulated platelets, but also that platelet-derived TAFI is capable of attenuating platelet-rich thrombus lysis in vitro independently of plasma TAFI using a novel thrombus lysis assay. Fluorescent ...
Inhibition of Fibrinolysis. For maintaining high fidelity regulation between coagulatory clotting and proteolytic fibrinolysis TAFI (Thrombin activatable fibrinolysis inhibitor) plays an important inhibitory role. Apart from this, four different forms of plasminogen activator inhibitors, denoted PAI-1 to PAI-4, are also known.. PAI-1, which is the most prominent form, is mainly synthesized in endothelial cells and stored in thrombocytes. Its release is concentrated to platelet rich clots leading to an increased thrombus resistance to fibrinolysis. Another fibrinolysis inhibitor is the plasmin inhibitor (α2-antiplasmin). FXIIIa makes it an initial clot stabilizer by rapidly and covalently binding this inhibitor to fibrin. The role of inhibiting plasmin is made directly by a 1:1-complex formation between plasmin and antiplasmin (PAP). PAP can be immunologically detected in plasma, and is therefore used as a diagnostic parameter for proving thrombosis.. Function of plasmin. The fibrinogen molecule ...
TAFI is a plasma protein assumed to be an important link between coagulation and fibrinolysis. The three-dimensional crystal structures of authentic mature bovine TAFI (TAFIa) in complex with tick carboxypeptidase inhibitor, authentic full lenght bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI), and recombinant human TAFI have recently been solved. In light of these recent advances, we have characterized authentic bovine TAFI biochemically and compared it to human TAFI. The four N-linked glycosylation sequons within the activation peptide were all occupied in bovine TAFI, similar to human TAFI, while the sequon located within the enzyme moiety of the bovine protein was non-glycosylated. The enzymatic stability and the kinetic constants of TAFIa differed somewhat between the two proteins, as did the isoelectric point of TAFI, but not TAFIa. Equivalent to human TAFI, bovine TAFI was a substrate for transglutaminases and could be proteolytically cleaved by trypsin or thrombin/solulin
Anti-Human TAFI Clone 3 - Detects Human Thrombin Activatable Fibrinolysis Inhibitor (TAFI) and activated TAFI. Mouse monoclonal of isotype IgG3.
Anti-Human TAFI Clone 1 - Detects Human Thrombin Activatable Fibrinolysis Inhibitor (TAFI) and activated TAFI. Mouse monoclonal of isotype IgG1.
Patients with hemophilia who have the same level of deficient factor(s) may express different severity of clinical presentation and bleeding tendency. Therefore a test which could determine overall hemostasis rather than simple concentration of a single deficient factor may correlate better with clinical phenotype in these patients.. The investigators will therefore study the usefulness of global hemostatic methods (endogenous thrombin potential (ETP), overall hemostatic potential (OHP), fibrin clot structure) and microparticles in the prediction of severity of bleeding and estimation of response to the treatment in patients with hemophilia.. Since hemophilia patients on prophylactic treatment virtually do not bleed, additional patients who are treated on demand only will be included enabling to study possible modulatory effects of different hemostatic factors (particularly prothrombotic and thrombin activatable fibrinolysis inhibitor (TAFI)) on clinical presentation. The investigators will ...
TY - JOUR. T1 - Heritability of hemostasis phenotypes and their correlation with type 2 diabetes status in Mexican Americans. AU - Warren, Diane M.. AU - Soria, José Manuel. AU - Souto, Juan Carlos. AU - Comuzzie, Anthony. AU - Fontcuberta, Jordi. AU - Blangero, John. AU - Maccluer, Jean W.. AU - Almasy, Laura. PY - 2005/2. Y1 - 2005/2. N2 - Hypercoagulation often occurs in type 2 diabetes, suggesting pleiotropy of the genes that influence disease liability and hemostasis-related phenotypes. To better understand the relationship between hemostasis and diabetes, we first used maximum-likelihood methods to estimate the relative contribution of additive genetic, measured environmental, and shared household effects to the normal variance of 16 hemostasis-related traits in 813 individuals participating in the San Antonio Family Heart Study. We estimated moderate to high heritabilities (0.20-0.60) for each phenotype. Von Willebrand factor (VWF), thrombin activatable fibrinolysis inhibitor, activated ...
Thrombomodulin (TM), CD141 or BDCA-3 is an integral membrane protein expressed on the surface of endothelial cells and serves as a cofactor for thrombin. It reduces blood coagulation by converting thrombin to an anticoagulant enzyme from a procoagulant enzyme. Thrombomodulin is also expressed on human mesothelial cell, monocyte and a dendritic cell subset. In humans, thrombomodulin is encoded by the THBD gene. The protein has a molecular mass of 74kDa, and consists of a single chain with six tandemly repeated EGF-like domains, a Serine/Threonine-rich spacer and a transmembrane domain. Thrombomodulin functions as a cofactor in the thrombin-induced activation of protein C in the anticoagulant pathway by forming a 1:1 stoichiometric complex with thrombin. This raises the speed of protein C activation thousandfold. Thrombomodulin-bound thrombin has procoagulant effect at the same time by inhibiting fibrinolysis by cleaving thrombin-activatable fibrinolysis inhibitor (TAFI, aka carboxypeptidase B2) ...
TY - CHAP. T1 - Plasmin-antiplasmin system. AU - Mutch, Nicola J.. AU - Booth, Nuala A.. PY - 2016/4/19. Y1 - 2016/4/19. N2 - Plasmin is the key enzyme involved in the dissolution of fibrin. It is produced from plasminogen, which is activated by a plasminogen activator; the two primary activators are tissue-type plasminogen activator (tPA) and urinary-type plasminogen activator (uPA), also called urokinase. The process is regulated by inhibitors, principally plasminogen activator inhibitor 1 (PAI-1), α2-antiplasmin (α2AP) and thrombin-activatable fibrinolysis inhibitor (TAFI). Crucial control is exerted by surfaces, such as fibrin or cells, with plasminogen activation not normally occurring in the circulation. Here we will consider the individual players of the fibrinolytic cascade and their specific locations and potential interactions. Key questions considered are the initiation of fibrinolysis and the most appropriate ways to measure abnormalities in disease situations.. AB - Plasmin is the ...
Free Online Library: Assay of procarboxypeptidase U, a novel determinant of the fibrinolytic cascade, in human plasma.(Enzymes and Protein Markers) by Clinical Chemistry; Fibrin Lysine
For the measurement of proCPU concentrations in human plasma, both functional and immunological assays are available.6,7,15,29⇓⇓⇓ The major advantage of immunological assays is that no activation of the zymogen is required, which makes ELISAs easy to perform. However, studies investigating a possible relationship between proCPU levels and cardiovascular diseases revealed conflicting results. ProCPU levels above the 90th percentile of population-based controls increased the risk for venous thrombosis compared with proCPU levels below the 90th percentile.30 In a case-control study of patients with stable angina pectoris, the plasma proCPU level in patients was significantly higher than in controls.31 In contrast, another study concluded that high levels of proCPU (above the 90th percentile) are protective for myocardial infarction.23. In this study, we describe the development of 2 ELISAs (T12D11/T28G6-HRP and T32F6/T9G12-HRP) for measurement of proCPU in plasma. When the antigen values ...
These highlights do not include all the information needed to use ARTISS safely and effectively. See full prescribing information for ARTISS ARTISS [Fibrin Sealant (Human)]For Topical Use OnlyFrozen solution and lyophilized powder for solution for topical applicationInitial U.S. Approval: ...
This invention relates to mutant forms of carboxypeptidase U with increased thermal stability relative to wild-type. In addition to the individual thermal stabilizing mutations identified (at position
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Fibrinolysis is a process that prevents blood clots from growing and becoming problematic. This process has two types: primary fibrinolysis and secondary fibrinolysis. The primary type is a normal body process, whereas secondary fibrinolysis is the breakdown of clots due to a medicine, a medical disorder, or some other cause. In fibrinolysis, a fibrin clot, the product of coagulation, is broken down. Its main enzyme plasmin cuts the fibrin mesh at various places, leading to the production of circulating fragments that are cleared by other proteases or by the kidney and liver. Plasmin is produced in an inactive form, plasminogen, in the liver. Although plasminogen cannot cleave fibrin, it still has an affinity for it, and is incorporated into the clot when it is formed. Tissue plasminogen activator (t-PA) and urokinase are the agents that convert plasminogen to the active plasmin, thus allowing fibrinolysis to occur. t-PA is released into the blood very slowly by the damaged endothelium of the ...
Semantic Scholar extracted view of The contribution of anti-Xa and anti-IIa activities to the profibrinolytic activity of low-molecular-weight heparins. by Concetta Tiziana Ammollo et al.
A sprayable preparation for accelerated hemostasis and optimized biochemical control of wound closure contains a powdery mixture of 15 to 60% by weight of thrombin, 5 to 80% by weight of a desiccating and stabilizing agent, viz., albumin, globulin and/or fibrinogen, and 1 to 10% by weight of a fibrinolysis inhibitor. The powdery mixture is suspended in a low-boiling, anhydrous solvent, which is used as a propellant. For effective wound closure and coverage, a spray jet of this suspension is directed onto the wound under evaporation of the solvent so that substantially only the dry, solid powdery mixture reaches the wound. This method of application by spraying is also disclosed.
Drotrecogin is a recombinant form of human Activated Protein C. It has antithrombotic and profibrinolytic effects and is used to reduce the mortality rate in adult patients with severe sepsis.
Hot‐start PCR is a technique that improves PCR performance by reducing nonspecific amplification during the initial setup stages of the PCR
DEPENDENCE OF TISSUES UPON TIIE VESSELS. 83. a nucleus may be distinguished within these bodies; and, even without entering into the history of their development, we discover that here too we have once more to deal with cellular elements of a stellate form. Bone therefore exhibits in its composition a tissue, containing, in an apparently altogether homogeneous basis-substance, peculiar, stellate bone-cells distributed in a very regular manner.. The intervals which exist between every two of the vessels in bone are often very considerable; whole systems of lamellae, beset with numerous bone-corpuscles, thrust themselves in between the medullary canals. Here it is certainly difficult to conceive the nutrition of so complicated an apparatus to depend upon the action of vessels some of them so remote, and especially so, to understand how every individual particle of this extensive compound mass can manage to maintain a special relation of nutrition to the vessels. For experience shows us that every ...
TY - JOUR. T1 - Activation of recombinant human protein C. AU - Lee, Timothy K.. AU - Bangalore, Neelesh. AU - Velander, William. AU - Drohan, William N.. AU - Lubon, Henryk. PY - 1996/5/1. Y1 - 1996/5/1. N2 - We have produced recombinant human Protein C (rHPC) in the milk of transgenic swine. After purification, we have analyzed the interaction of the zymogen with Protac, thrombin/thrombomodulin and thrombin alone. The amidolytic and anticoagulant activities of rAPC after Protac activation were ~80% those of its human plasma counterpart. Upon the excision of the activation peptide by thrombin/thrombomodulin complex, both the natural and recombinant activation products had similar enzymatic and biological activities. This. observation can be attributed to the difference in the mechanism of action between the two activators and structural differences between HPC and rHPC.. AB - We have produced recombinant human Protein C (rHPC) in the milk of transgenic swine. After purification, we have ...
Blood coagulation and fibrinolytic factors have been measured in 13 patients treated by liver transplantation. During operation intravascular coagulation and fibrinolysis were increased, but seldom to a degree which would cause abnormal bleeding. Measurement of the catabolism of radioactive fibrinogen showed that increased intravascular coagulation continued for long periods after the operation. Despite secondarily increased fibrinolysis, there was a high incidence of thrombosis. Treatment with anticoagulants or with fibrinolysis inhibitors may be valuable in these patients.. ...
The present study demonstrates that thrombin, the central protease of the coagulation cascade, can be functionally imaged in vivo by using a novel NIR thrombin-activatable reporter. In vitro experiments first confirmed that the probe was specifically activated by endogenous thrombin within blood. In experimental murine thrombosis models, thrombin activation of the probe resulted in focal NIRF signal enhancement in occlusive and nonocclusive thrombi. Thrombin activity was detected within acute and subacute thrombi with the use of probe injections at clinically relevant time points, did not require preinjection of the probe, and could be rapidly detected in vivo by fluorescence reflectance imaging systems.. Although in vitro thrombin activity has been detected for many years with the use of chromogenic or fluorogenic substrates,18,19⇓ current experimental results now show that thrombin activity can be imaged in vivo by using the NIRF-activatable probe scheme previously developed in our ...
TY - JOUR. T1 - Fibrinolysis és érbetegségek.. AU - Udvardy, M.. AU - Boda, Z.. PY - 1996/8/25. Y1 - 1996/8/25. N2 - A wide array of in vitro fibrinolysis tests had been performed for a long period, suggesting defective fibrinolysis, mainly impaired tPA response and reserve as major, frequent abnormality, predecessor or causative factor of venous thromboembolism. However, these abnormalities were troublesome to reproduce, and more recently fibrinolytic activators and inhibitors received growing attention as rather atherogenic and less thrombogenic risk factors. Even if it is still not settled, lipoprotein(a) may interfere with fibrinolysis, and seems to carry atherogenic risk, too. The genetic polymorphism of fibrinogen, plasminogen, PAI-1 and some other compounds modifying circulating fibrinogen levels are also discussed in this review.. AB - A wide array of in vitro fibrinolysis tests had been performed for a long period, suggesting defective fibrinolysis, mainly impaired tPA response and ...
Annexin II is thought to serve as a profibrinolytic coreceptor for both plasminogen and tissue plasminogen activator on the surface
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Stefan Wiehr is the author of this article in the Journal of Visualized Experiments: Non-invasive In Vivo Fluorescence Optical Imaging of Inflammatory MMP Activity Using an Activatable Fluorescent Imaging Agent
TY - JOUR. T1 - The activation pathway of procarboxypeptidase B from porcine pancreas: Participation of the active enzyme in the proteolytic processing. AU - Villegas, Virtudes. AU - Vendrell, Josep. AU - Avilés, Francesc X.. PY - 1995/1/1. Y1 - 1995/1/1. N2 - The activation process of porcine pancreatic procarboxypeptidase B (pro‐CPB) has been studied in detail by a number of complementary methodologies, and a description of the molecular events that lead to the generation of active carboxypeptidase B (CPB) has been deduced. The generated CPB participates in the degradation of its own activation segment by excising C‐terminal residues from fragments produced by tryptic proteolysis. The trimming action of CPB is, however, not essential for the release of a fully functional enzyme, in contrast to what was previously reported for porcine procarboxypeptidase A (pro‐CPA). In the model presented here, the activation process is solely dependent on the first tryptic cleavage, at the limit ...
TY - JOUR. T1 - Ambivalent roles of carboxypeptidase B in the lytic susceptibility of fibrin. AU - Kovács, András. AU - Szabó, László. AU - Longstaff, Colin. AU - Tenekedjiev, Kiril. AU - Machovich, Raymund. AU - Kolev, Krasimir. PY - 2014/1/1. Y1 - 2014/1/1. N2 - Background Removal of C-terminal lysine residues that are continuously exposed in lysing fibrin is an established anti-fibrinolytic mechanism dependent on the plasma carboxypeptidase TAFIa, which also removes arginines that are exposed at the time of fibrinogen clotting by thrombin. Objective To evaluate the impact of alterations in fibrin structure mediated by constitutive carboxypeptidase activity on the function of fibrin as a template for tissue plasminogen activator-(tPA) induced plasminogen activation and its susceptibility to digestion by plasmin. Methods and results We used the stable carboxypeptidase B (CPB), which shows the same substrate specificity as TAFIa. If 1.5 - 6 μM fibrinogen was clotted in the presence of 8 ...
TGF beta, in flip, may well maximize the synthesis of PAI 1 in endothelial cells. These mechanisms may describe, not less than in component, the enhanced plasma levels of PAI one in BD sufferers be result in they present systemic activation of coagulation and improved thrombin manufacturing in response to stimulus. Enhanced levels of PAI 1 can improve the clot formation velocity and clot stability due to the rapid and irre versible blockage in the protease action of tPA, the key plasminogen activator. Our final results agree with this particular observation given that we found a substantial correl ation among antigenic ranges of PAI one and INTEM CFT, INTEM and INTEM MCF, which points to PAI 1 like a vital aspect while in the procoagulant state observed in BD individuals by this test.. Regardless of the fact that an associ ation between ranges of PAI 1 and thrombosis in BD hasnt been reported, relief from vascular events and oral ulcers right after treatment method with profibrinolytic agents ...
There is disclosed a process of forming reinforcements, baffles and seals having malleable carriers. The process typically includes application of an activatable material to a malleable carrier and contouring of the activatable material the malleable carrier or both.
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If the thrombotic tendency plays a significant role in the etiology of psychosis, one would expect to find ischemic brain injuries in neuroimaging studies, but it does not happen. Therefore, if there is a correlation between thrombotic tendency-hypofibrinolysis and psychosis it is likely to occur at the biochemical level, such as in neuronal transmission.. The investigators hypothesis is that mechanisms that inhibit tissue plasminogen activator (t-PA) and therefore promote hypofibrinolysis, are directly or indirectly involved in the genesis of psychosis, because t-PA participates in neuronal plasticity and low t-PA levels are related to dementia.. Hypofibrinolysis due to t-PA inhibition can be seen in:. ...
Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for this gene and its promoter region. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jun 2013 ...
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TY - JOUR. T1 - Plasmin catalyzed fibrinolysis as quantified by a new kinetic method. AU - Sazonova, I. V.. AU - Sirovskava, S. F.. AU - Aisina, R. B.. AU - Varfolomevev, S. D.. PY - 1996/12/1. Y1 - 1996/12/1. N2 - Kinetics fibrinolysis by plasmin (Pro) was studied by a new method which allowed to describe quantitatively the clot lysis reaction. Cylindrical fibrin (Fn) clots (0.9 ml) were formed in glass tubes of different diameters. After addition of Pm (5 nM1 μM) in buffer over the clots, the lysis kinetics at 37°C was traced by decrease of clot column height with catetometer. Linear rate of lysis (VI) was measured as tangent of the clot boundary movement in time (mm/min). Because of fibrin surface square (S) did not change during the lysis, the mass rates of lysis (VM, M/min) were calculated from equation: VM=vI·S·[Fn]/v, where [Fn] was Fn concentration in clot, v was liquid phase volume. Dependences of VM on the Pm and Fn concentrations, as well as on S and shaking rate were obtained. It ...
Sigma-Aldrich offers abstracts and full-text articles by [Ivan S Alferiev, Radhika Iyer, Jamie L Croucher, Richard F Adamo, Kehan Zhang, Jennifer L Mangino, Venkatadri Kolla, Ilia Fishbein, Garrett M Brodeur, Robert J Levy, Michael Chorny].
Kerstin Fuchs is the author of this article in the Journal of Visualized Experiments: Non-invasive In Vivo Fluorescence Optical Imaging of Inflammatory MMP Activity Using an Activatable Fluorescent Imaging Agent
0018]According to the invention, this object is achieved by a fibrinogen-based tissue adhesive which is characterized in that it comprises an admixed elastase inhibitor. For, surprisingly, it has been shown that the fibrinolysis process cannot only be prevented by inhibiting plasmin or by inhibiting the activation of plasminogen to plasmin, but also by elastase inhibitors or by inhibitors whose fibrinolysis-inhibiting action is mainly based on a non-plasmin fibrinolysis mechanism, respectively. For reasons of simplicity, such non-plasminogen fibrinolysis inhibitors are encompassed by the term elastase inhibitor for the purposes of the present invention. It has been speculated that besides the plasmin-mediated fibrinolysis, also further fibrinolytic processes might exist which are not based on plasmin (e.g. a lysosomal process; cf. Simon at al., BLOOD 82 (8) (1993), pp. 2414-2422), and which cannot be substantially inhibited by aprotinin; yet, it has also been shown that this non-plasmin ...
Serial changes in coagulation and fibrinolysis studied among 42 patients admitted to hospital with a wide variety of injuries are reported. The first hours after trauma are dominated by an acceleration of fibrinolysis (clot lysis) and clotting time which are often followed by an abrupt rebound to prolonged fibrinolysis and normal clotting. Evidence is presented that acceleration of fibrinolysis is due to flooding of the circulation by plasminogen activator and that prolongation is probably due to an inhibitor. A prolonged prothrombin time, increased prothrombin consumption index, an acceleration of the heparin-retarded clotting time, and a fall in the platelet count are also frequent during the first hours after injury. There is evidence also of an early deficiency in factor V and the onset of a fall in factor VII and prothrombin.. The following days are characterized by continued prolongation of fibrinolysis, a lengthening of clotting time, and an increased prothrombin consumption index ...
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A method of microdissection which involves: forming an image field of cells of the tissue sample utilizing a microscope, identifying at least one zone of cells of interest from the image field of cells which at least one zone of cells of interest includes different types of cells than adjacent zones of cells, and extracting the at least one zone of cells of interest from the tissue sample. The extraction is achieved by contacting the tissue sample with a transfer surface that can be selectively activated so that regions thereof adhere to the zone of cells of interest to be extracted. The transfer surface includes an activatable adhesive layer which provides chemical or electrostatic adherence to the selected regions of the tissue sample. After the transfer surface is activated the transfer surface and tissue sample are separated. During separation the zone of cells of interest remains adhered to the transfer surface and is thus separated from the tissue sample.
Discontinuous transcription has been described for different mammalian cell lines and numerous promoters. However, our knowledge of how the activity of individual promoters is adjusted by dynamic signaling inputs from transcription factors is limited. To address this question, we characterized the activity of selected target genes that are regulated by pulsatile accumulation of the tumor suppressor p53 in response to ionizing radiation. We performed time-resolved measurements of gene expression at the single-cell level by smFISH and used the resulting data to inform a mathematical model of promoter activity. We found that p53 target promoters are regulated by frequency modulation of stochastic bursting and can be grouped along three archetypes of gene expression. The occurrence of these archetypes cannot solely be explained by nuclear p53 abundance or promoter binding of total p53. Instead, we provide evidence that the time-varying acetylation state of p53s C-terminal lysine residues is ...
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Recently, researchers at Agroscope Changins-Wädenswil ACW in Switzerland have, through conventional breeding methods, developed new soybean varieties with a lower trypsin inhibitor level.
The coagulation-fibrinolysis system is considered to be an important factor in the growth and spread of tumors (Kodama, 1974; Kinjo, 1978). At the advancing border of the tumors, deposition of fibrin...
... some carboxypeptidase; low tyrosinase Aesthetics: pleasant fragrance; accumulation of flavoring compounds Color: low production ...
MPI Carboxypeptidase N deficiency; 212070; CPN1 Carcinoid tumors, intestinal; 114900; SDHD Cardiac arrhythmia, ankyrin-B- ...
... carboxypeptidase A2 (CPA2), and carboxypeptidase B. This subfamily includes 6 carboxypeptidase A-like enzymes, numbered 1-6. ... Carboxypeptidase A3 (mast cell carboxypeptidase A), also known as CPA3, is an enzyme which in humans is encoded by the CPA3 ... and comparison of the protein with mouse mast cell carboxypeptidase A and rat pancreatic carboxypeptidases". Proceedings of the ... Huang H, Reed CP, Zhang JS, Shridhar V, Wang L, Smith DI (June 1999). "Carboxypeptidase A3 (CPA3): a novel gene highly induced ...
Carboxypeptidase A5 is an enzyme that in humans is encoded by the CPA5 gene. Carboxypeptidases have functions ranging from ... "Entrez Gene: CPA5 carboxypeptidase A5". Human CPA5 genome location and CPA5 gene details page in the UCSC Genome Browser. ... Members of the A/B subfamily of carboxypeptidases, such as CPA5, contain an approximately 90-amino acid pro region that assists ... 2003). "The imprinted region on human chromosome 7q32 extends to the carboxypeptidase A gene cluster: an imprinted candidate ...
Carboxypeptidase A4 is an enzyme that in humans is encoded by the CPA4 gene. This gene is a member of the carboxypeptidase A/B ... "Entrez Gene: CPA4 carboxypeptidase A4". Human CPA3 genome location and CPA3 gene details page in the UCSC Genome Browser. Human ... 2005). "Detailed molecular comparison between the inhibition mode of A/B-type carboxypeptidases in the zymogen state and by the ... 2003). "The novel imprinted carboxypeptidase A4 gene ( CPA4) in the 7q32 imprinting domain". Hum. Genet. 112 (3): 220-6. doi: ...
... (EC 3.4.15.5, dipeptidyl carboxypeptidase (Dcp), dipeptidyl carboxypeptidase) is an enzyme. It ... Yaron, A. (1976). "Dipeptidyl carboxypeptidase from Escherichia coli". Methods Enzymol. 45: 599-610. doi:10.1016/s0076-6879(76) ...
The structure of carboxypeptidase A. VI. Some Results at 2.0-A Resolution, and the Complex with Glycyl-Tyrosine at 2.8-A ... The Structure of Carboxypeptidase A, IV. Prelimitary Results at 2.8 A Resolution, and a Substrate Complex at 6 A Resolution. ... The structure of carboxypeptidase A. VII. The 2.0-angstrom resolution studies of the enzyme and of its complex with ... "The Structure of Carboxypeptidase A. III. Molecular Structure at 6 A Resolution," J Mol. Biol. 19, 423-441 (1966). Ludwig, M. L ...
Retinoid-inducible serine carboxypeptidase is an enzyme that in humans is encoded by the SCPEP1 gene. GRCh38: Ensembl release ... "Entrez Gene: SCPEP1 serine carboxypeptidase 1". Robb GB, Rana TM (2007). "RNA helicase A interacts with RISC in human cells and ... "Cloning of a novel retinoid-inducible serine carboxypeptidase from vascular smooth muscle cells". J Biol Chem. 276 (36): 34175- ...
Probable serine carboxypeptidase CPVL is an enzyme that in humans is encoded by the CPVL gene. The "CPVL" gene is expressed ... "Entrez Gene: CPVL carboxypeptidase, vitellogenic-like". Harris J, Schwinn N, Mahoney JA, Lin HH, Shaw M, Howard CJ, da Silva RP ... Although the primary sequence of CPVL bears every hallmarks of a serine carboxypeptidase, the enzymatic function of CPVL has ... The designation of CPVL is a true serine carboxypeptidase. Although the primary sequence displays the expected serine ...
1968 - Papain 1969 - Carboxypeptidase A is a zinc metalloprotease. Its crystal structure (PDB file 1CPA) showed the first ... Rees DC, Lipscomb WN (1982). "Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A ... Later a small protein inhibitor of carboxypeptidase was solved (PDB file 4CPA) that mechanically stops the catalysis by ... "The structure of carboxypeptidase A, VII. The 2.0-Å resolution studies of the enzyme and of its complex with glycyltyrosine, ...
... produces streptomycin II and carboxypeptidase. Sholkamy, Essam; Ahmad, Maged; Manal Yaser, Manal; Ali ... "Carboxypeptidase from Streptomyces bikiniensis: Primary structure, isolation, and properties". Biochemistry (Moscow). 75 (8): ...
Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene. Carboxypeptidase N is a plasma ... 2000). "Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not". J. Immunol. 165 (2 ... "Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N". Microbiol. Immunol. 46 (2): 131-4. doi: ... "Entrez Gene: CPN1 carboxypeptidase N, polypeptide 1". Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets ...
Matthews KW, Mueller-Ortiz SL, Wetsel RA (Jan 2004). "Carboxypeptidase N: a pleiotropic regulator of inflammation". Molecular ...
"Entrez Gene: CPN2 carboxypeptidase N, polypeptide 2". Human CPN2 genome location and CPN2 gene details page in the UCSC Genome ... Carboxypeptidase N subunit 2 is an enzyme that in humans is encoded by the CPN2 gene. GRCh38: Ensembl release 89: ... Riley DA, Tan F, Miletich DJ, Skidgel RA (Apr 1999). "Chromosomal localization of the genes for human carboxypeptidase D (CPD) ... "Amino acid sequence of the N-terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase N: ...
Alanine aminopeptidase Carboxypeptidase PDB: 3QNF​: Vollmar, M.; Kochan, G.; Krojer, T.; Harvey, D.; Chaikuad, A.; Allerston, C ...
Carboxypeptidase M is an enzyme that in humans is encoded by the CPM gene. The protein encoded by this gene is a membrane-bound ... "Entrez Gene: CPM carboxypeptidase M". Human CPM genome location and CPM gene details page in the UCSC Genome Browser. Fujiwara ... 1995). "Distribution of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and ... 1998). "Membrane-bound carboxypeptidase-M is expressed on human ovarian follicles and corpora lutea of menstrual cycle and ...
Lyons PJ, Callaway MB, Fricker LD (March 2008). "Characterization of carboxypeptidase A6, an extracellular matrix peptidase". ... carboxypeptidase A6 (CPA6), and angiotensin-converting enzyme (ACE). These enzymes are sometimes referred to as enkephalinases ... the resulting intermediates are further reduced by the enzyme carboxypeptidase E (CPE; previously known as enkephalin ...
Lyons PJ, Callaway MB, Fricker LD (March 2008). "Characterization of carboxypeptidase A6, an extracellular matrix peptidase". ... They include: Aminopeptidase N (APN) Neutral endopeptidase (NEP) Dipeptidyl peptidase 3 (DPP3) Carboxypeptidase A6 (CPA6) ...
The digestive enzyme carboxypeptidase became the second known zinc-containing enzyme in 1955. Zinc is the fourth most common ... Carboxypeptidase cleaves peptide linkages during digestion of proteins. A coordinate covalent bond is formed between the ... Two examples of zinc-containing enzymes are carbonic anhydrase and carboxypeptidase, which are vital to the processes of carbon ...
Probable carboxypeptidase X1 is an enzyme that in humans is encoded by the CPXM1 gene. The protein encoded by this gene is a ... "Entrez Gene: CPXM1 carboxypeptidase X (M14 family), member 1". Human CPXM1 genome location and CPXM1 gene details page in the ... member of the M14 family of zinc carboxypeptidases; however, the protein has no detectable carboxypeptidase activity. The ...
Carboxypeptidase, which is a protease that takes off the terminal amino acid group from a protein ...
Cloning and functional expression as a captopril-insensitive carboxypeptidase". The Journal of Biological Chemistry. 275 (43): ... "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9". Circulation ... "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9". Circulation ... "Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase". The Journal of Biological ...
CPN2: Carboxypeptidase N subunit 2. *CPOX: coproporphyrinogen oxidase (coproporphyria, harderoporphyria). *DPPA2: Developmental ...
... (EC 3.4.18.1, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, ... lysosomal carboxypeptidase B) is an enzyme. This enzyme catalyses the following chemical reaction Release of C-terminal amino ... A cysteine protease with unique carboxypeptidase activity". Biochemistry. 38 (39): 12648-12654. doi:10.1021/bi991371z. PMID ...
It is an exopeptidase with strict carboxypeptidase activity, while most other cathepsins are endopeptidases. Cathepsin Z has an ... A cysteine protease with unique carboxypeptidase activity". Biochemistry. 38 (39): 12648-54. doi:10.1021/bi991371z. PMID ...
There is evidence that the receptor in the closely related duck hepatitis B virus is carboxypeptidase D. The virions bind to ... Tong S, Li J, Wands JR (1999). "Carboxypeptidase D is an avian hepatitis B virus receptor" (PDF). Journal of Virology. 73 (10 ...
Rees, DC; Lewis M (1983). "Refined crystal structure of carboxypeptidase a at 1.54 Å resolution". Journal of Molecular Biology ...
... is a member of carboxypeptidase A protein family. The protein may function as a transcriptional repressor ... Muise AM, Ro HS (1999). "Enzymic characterization of a novel member of the regulatory B-like carboxypeptidase with ... Tumelty KE, Smith BD, Nugent MA, Layne MD (2014). "Aortic carboxypeptidase-like protein (ACLP) enhances lung myofibroblast ... Song L, Fricker LD (1997). "Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase". The Journal ...
Carboxypeptidase Z is an enzyme that in humans is encoded by the CPZ gene. This gene encodes a member of the ... "Entrez Gene: CPZ carboxypeptidase Z". Human CPZ genome location and CPZ gene details page in the UCSC Genome Browser. Reznik SE ... This enzyme displays carboxypeptidase activity towards substrates with basic C-terminal residues. It is most active at neutral ... Novikova EG, Reznik SE, Varlamov O, Fricker LD (2000). "Carboxypeptidase Z is present in the regulated secretory pathway and ...
Carboxypeptidases (CP), carboxypeptidase N (CPN) and carboxypeptidase R (CPR), have been reported as a protease, which can ... CPR (identical to carboxypeptidase U [CPU], plasma carboxypeptidase B [plasma CPB]) has also been described as an inhibitor of ... Komura, H., Obata, K., Campbell, W. et al. Measurement of carboxypeptidase R by colorimetric assay. Crit Care 6, P124 (2002). ...
Carboxypeptidase U / blood*. Endothelial Cells. Enzyme-Linked Immunosorbent Assay. Female. Hemostasis. Humans. Hypertension / ... 0/Antihypertensive Agents; 0/Biological Markers; EC 3.4.17.20/Carboxypeptidase U From MEDLINE®/PubMed®, a database of the U.S. ...
This invention relates to mutant forms of carboxypeptidase U with increased thermal stability relative to wild-type. In ... Although crystal structures for other carboxypeptidases, e.g., carboxypeptidase B (CPB) have been solved. The crystal structure ... plasma carboxypeptidase B or carboxypeptidase R. The term CPU is used herein. ProCPU is converted to CPU during coagulation or ... Carboxypeptidase U (CPU, EC 3.4.17.20) is a Zn metallopeptidase that circulates in plasma in a zymogen form, proCPU. CPU has ...
... which confirmed its identity as plasma carboxypeptidase B (7). Determination of carboxypeptidase activity. The carboxypeptidase ... I. Active carboxypeptidase B. Clin Chem 1985;31: 1294-300. (12.) Wang W, Hendriks D, Scharpe S. Carboxypeptidase U: a plasma ... Characterization of a carboxypeptidase in human serum distinct from carboxypeptidase N. J Clin Chem Clin Biochem 1989;27:277-85 ... CPU activity was calculated by subtracting the carboxypeptidase activity without activation from the carboxypeptidase activity ...
Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N. J Clin Chem Clin Biochem. 1989; 27: 277 ... Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone ... Vanhoof G, Wauters J, Schatteman K, Hendriks D, Goossens F, Bossuyt P, Scharpe S. The gene for human carboxypeptidase U (CPU)-a ... Carboxypeptidase U (CPU) or activated thrombin activatable fibrinolysis inhibitor (TAFIa) is generated from its zymogen proCPU ...
The three-dimensional crystal structures of authentic mature bovine TAFI (TAFIa) in complex with tick carboxypeptidase ... Campbell WD, Lazoura E, Okada N, Okada H: Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N ... Wang W, Hendriks DF, Scharpe SS: Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen. J Biol Chem ... The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double ...
Carboxypeptidase T (EC 3.4.17.18, CPT) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction ... an extracellular carboxypeptidase of thermophilic actinomycetes - a remote analog of animal carboxypeptidases". Biochemistry ( ... Carboxypeptidase T at the US National Library of Medicine Medical Subject Headings (MeSH) ... "Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris". Eur. J. Biochem. 208: 281-288. doi:10.1111/j.1432- ...
D-alanyl-D-alanine-cleaving carboxypeptidase, DD-carboxypeptidase, G enzyme, DD-carboxypeptidase-transpeptidase) is an enzyme. ... Zinc D-Ala-D-Ala carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... Zinc D-Ala-D-Ala carboxypeptidase (EC 3.4.17.14, Zn2+ G peptidase, D-alanyl-D-alanine hydrolase, ... "The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G". ...
Peptidase M14 Carboxypeptidase (CP) B2 (CPB2, also known as plasma carboxypeptidase B, carboxypeptidase U, CPU, and thrombin- ... Carboxypeptidase U (TAFIa): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for ...
Definition of carboxypeptidase A. Provided by Stedmans medical dictionary and Drugs.com. Includes medical terms and ... carboxypeptidase A. Pronunciation: kar-bok′sē-pep′ti-dās. Definition: A hydrolase that releases C-terminal amino acids, with ...
... an alanine carboxypeptidase bradykinin is broken down among other enzymes by carboxypeptidase N D-Ala carboxypeptidase is a ... The first carboxypeptidases studied were those involved in the digestion of food (pancreatic carboxypeptidases A1, A2, and B). ... Carboxypeptidase E Carboxypeptidase A Enzyme category EC number 3.4 Thrombin-activatable fibrinolysis inhibitor aka plasma ... In the case of pancreatic carboxypeptidase A, the inactive zymogen form - pro-carboxypeptidase A - is converted to its active ...
Escherichia coli mutants defective in dipeptidyl carboxypeptidase. C E Deutch and R L Soffer ... Two independent mutants of Escherichia coli deficient in dipeptidyl carboxypeptidase activity (Dep-) were isolated after ... mutants may prove useful for delineating the regulation and cellular function of dipeptidyl carboxypeptidases in higher ... a potent inhibitor of mammalian dipeptidyl carboxypeptidase (angiotensin-converting enzyme, peptidyl dipeptidase, EC 3.4.15.1 ...
carboxypeptidase synonyms, carboxypeptidase pronunciation, carboxypeptidase translation, English dictionary definition of ... carboxypeptidase. n. Any of several enzymes that catalyze the hydrolysis of the terminal amino acid of a polypeptide from the ... Related to carboxypeptidase: dipeptidase, Carboxypeptidase B, Carboxypeptidase E, Carboxypeptidase c, carboxypeptidase G2 car· ... Carboxypeptidase - definition of carboxypeptidase by The Free Dictionary https://www.thefreedictionary.com/carboxypeptidase ...
This entry represents the carboxypeptidase domain found in carboxypeptidase (CP) E (CPE, also known as carboxypeptidase H, and ... Primary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family.. J. ... The carboxypeptidase A family can be divided into four subfamilies: M14A (carboxypeptidase A or digestive), M14B ( ... Carboxypeptidase E in the mouse placenta.. Differentiation 74 648-60 2006. Rawlings ND, Barrett AJ. Evolutionary families of ...
... carboxypeptidase II, lysyl-D-alanine carboxypeptidase, L-lysyl-D-alanine carboxypeptidase, LD-carboxypeptidase) is an enzyme. ... Muramoyltetrapeptide carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... Metz, R.; Henning, S.; Hammes, W.P. (1986). "LD-Carboxypeptidase activity in Escherichia coli. II. Isolation, purification and ... DasGupta, H.; Fan, D.P. (1979). "Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium ...
Low P.S., Yuan J. (1996) Rapid Epitope Mapping by Carboxypeptidase Digestion and Immunoblotting. In: Walker J.M. (eds) The ... Hayashi, R., Moore, S., and Stein, W. H. (1973) Carboxypeptidase from yeast:Large scale preparation and the application to COOH ...
Preferential cleavage:
Chowdhury C, Nayak TR, Young KD et al (2010) A weak DD-carboxypeptidase activity explains the inability of PBP 6 to substitute ... Pal S., Ghosh A.S. (2019) PBP Isolation and DD-Carboxypeptidase Assay. In: Biswas I., Rather P. (eds) Acinetobacter baumannii. ... PBPs are also involved in PG remodeling by catalyzing DD-carboxypeptidase (DD-CPase) and endopeptidase reactions. Though the ... Ghosh AS, Chowdhury C, Nelson DE (2008) Physiological functions of D-alanine carboxypeptidases in Escherichia coli. Trends ...
Similar to that of carboxypeptidase A EC 3.4.17.1, but with a preference for bulkier C-terminal residues. UniProt ...
Lysosomal protective protein, EC 3.4.16.5 (Carboxypeptidase C) (Carboxypeptidase L) (Cathepsin A) (Protective protein cathepsin ... CarboxypeptidaseUniRule annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system, ... tr,U3KQU6,U3KQU6_HUMAN Carboxypeptidase OS=Homo sapiens OX=9606 GN=CTSA PE=1 SV=1 ...
Compare carboxypeptidase A4 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, ... carboxypeptidase A4 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established antibody-based tool for ... Your search returned 53 carboxypeptidase A4 ELISA ELISA Kit across 8 suppliers. ...
Rabbit polyclonal Carboxypeptidase A antibody validated for WB and tested in Human, Mouse, Rat and Pig. Immunogen corresponding ... All lanes : Anti-Carboxypeptidase A antibody (ab63806) at 4 µg/ml. Lane 1 : Jurkat cell lysate. Lane 2 : Jurkat cell lysate. ... Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys ...
Compare carboxypeptidase, vitellogenic like ELISA Kits from leading suppliers on Biocompare. View specifications, prices, ... carboxypeptidase, vitellogenic like ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a widely used application for ... Your search returned 24 carboxypeptidase, vitellogenic like ELISA ELISA Kit across 3 suppliers. ...
Anti-Carboxypeptidase Y antibody conjugated to Biotin validated for WB, ELISA, IM, Dot. Immunogen corresponding to full length ... This antibody has been assayed against 1.0µg of Carboxypeptidase Y in a standard capture ELISA using Peroxidase conjugated ...
Human glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) is an established marker for prostate-cancer diagnosis as well as a ... A high-resolution structure of ligand-free human glutamate carboxypeptidase II.. Barinka C1, Starkova J, Konvalinka J, ... A high-resolution structure of ligand-free human glutamate carboxypeptidase II. Acta Crystallogr Sect F Struct Biol Cryst ... A high-resolution structure of ligand-free human glutamate carboxypeptidase II. Acta Crystallogr Sect F Struct Biol Cryst ...
Potent inhibitor of pancreatic carboxypeptidase A with a Ki of 27 nM, and of the serine proteases trypsin, chymotrypsin and ...
Downloading a figure as powerpoint requires a browser with javascript support. Enable javascript and try again For help please contact [email protected] ...
Characterization of a carboxypeptidase in human serum distinct from carboxypeptidase N. J Clin Chem Clin Biochem 1989. 27:277- ... Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen. J Biol Chem 1994. 269:15937-15944. View this ... potato carboxypeptidase inhibitor (PCI); plasma carboxypeptidase N (CpN); activated protein C (APC); embryonic stem (ES). ... Plasma carboxypeptidases as regulators of the plasminogen system. J Clin Invest 1995. 96:2534-2538. View this article via: JCI ...
Antibodies to human carboxypeptidase B and methods of use thereof. US5593674. Apr 27, 1995. Jan 14, 1997. Genentech, Inc.. ... Carboxypeptidases are proteases that hydrolyze the peptide bonds at the carboxy-terminal end of a chain of amino acids and have ... Plasma carboxypeptidase. US5837458. May 20, 1996. Nov 17, 1998. Maxygen, Inc.. Methods and compositions for cellular and ... Regulation of human zinc carboxypeptidase b-like protein. US20080003673 *. Sep 6, 2005. Jan 3, 2008. Alejandro Abuin. Novel ...
Browse our Carboxypeptidase M Lysate catalog backed by our Guarantee+. ... We offer Carboxypeptidase M Lysates for use in common research applications: Western Blot. Each Carboxypeptidase M Lysate is ... Our Carboxypeptidase M Lysates can be used in a variety of model species: Human. Use the list below to choose the ... Carboxypeptidase M lysate, CPM lysate, EC 3.4.17 lysate, EC 3.4.17.12 lysate ...
Browse our Carboxypeptidase M Protein catalog backed by our Guarantee+. ... Carboxypeptidase M Proteins. We offer Carboxypeptidase M Peptides and Carboxypeptidase M Proteins for use in common research ... Our Carboxypeptidase M Peptides and Carboxypeptidase M Proteins can be used in a variety of model species: Human. Use the list ... Each Carboxypeptidase M Peptide and Carboxypeptidase M Protein is fully covered by our Guarantee+, to give you complete peace ...
Cytosolic carboxypeptidase 4 (EC:3.4.17.-*Search proteins in UniProtKB for this EC number. ... sp,Q96MI9,CBPC4_HUMAN Cytosolic carboxypeptidase 4 OS=Homo sapiens OX=9606 GN=AGBL1 PE=1 SV=3 ...
Carboxypeptidase A1 Polyclonal Antibody from Invitrogen for Western Blot and Immunohistochemistry (Paraffin) applications. This ... Protein Aliases: Carboxypeptidase A1; carboxypeptidase A1 (pancreatic); CPA; pancreatic carboxypeptidase A Gene Aliases: CPA; ... Cite Carboxypeptidase A1 Polyclonal Antibody. The following antibody was used in this experiment: Carboxypeptidase A1 ... A synthetic peptide derived from the internal region of human CARBOXYPEPTIDASE A1 ...
NOS1AP regulates dendrite patterning of hippocampal neurons through a carboxypeptidase E-mediated pathway.. Carrel D1, Du Y, ... NOS1AP Regulates Dendrite Patterning of Hippocampal Neurons through a Carboxypeptidase E-Mediated Pathway ... NOS1AP Regulates Dendrite Patterning of Hippocampal Neurons through a Carboxypeptidase E-Mediated Pathway ... NOS1AP Regulates Dendrite Patterning of Hippocampal Neurons through a Carboxypeptidase E-Mediated Pathway ...
anti-Carboxypeptidase A6 Antikörper The protein encoded by CPA6 belongs to the family of carboxypeptidases, which catalyze the ... Carboxypeptidase A6 (CPA6) Antigen-Profil Protein Überblick The protein encoded by this gene belongs to the family of ... anti-Carboxypeptidase A6 (CPA6) (AA 285-315) Antikörper Primary Antibody CPA6 Reaktivität: Human WB Wirt: Kaninchen Polyclonal ... anti-Carboxypeptidase A6 (CPA6) Antikörper Primary Antibody CPA6 Reaktivität: Human WB Wirt: Kaninchen Polyclonal unconjugated ...
carboxypeptidase H. Known as: Enkephalin-Forming Carboxypeptidase, Enkephalin Synthesizing Carboxypeptidase, Carboxypeptidase E ... Carboxypeptidase E mediates palmitate-induced beta-cell ER stress and apoptosis.. *Kristin D. Jeffrey, Emilyn U. Alejandro, +7 ... Carboxypeptidase E Is a Regulated Secretory Pathway Sorting Receptor: Genetic Obliteration Leads to Endocrine Disorders in ... Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity ...
  • also known as carboxypeptidase R, plasma carboxypeptidase B, or TAFIa). (thefreelibrary.com)
  • The three-dimensional crystal structures of authentic mature bovine TAFI (TAFIa) in complex with tick carboxypeptidase inhibitor, authentic full lenght bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI), and recombinant human TAFI have recently been solved. (biomedcentral.com)
  • Campbell and co-workers (5, 6) confirmed these findings and called the enzyme carboxypeptidase R, where "R" represents arginine. (thefreelibrary.com)
  • CPR (identical to carboxypeptidase U [CPU], plasma carboxypeptidase B [plasma CPB]) has also been described as an inhibitor of fibrinolysis, and termed TAFI (thrombin activatable fibrinolysis inhibitor). (biomedcentral.com)
  • We first reported in 1988 on the presence of a labile carboxypeptidase activity in fresh human serum that interfered with the assay of CPN (1-3). (thefreelibrary.com)
  • This name, however, is rather confusing because the term "plasma carboxypeptidase B" had long been used as a synonym for plasma carboxypeptidase N (9). (thefreelibrary.com)
  • Carboxypeptidases (CP), carboxypeptidase N (CPN) and carboxypeptidase R (CPR), have been reported as a protease, which can cleave carboxy-terminal arginine or lysine residues from biologically active peptides, such as C3a and C5a, and regulate their activity. (biomedcentral.com)
  • Carboxypeptidase T ( EC 3.4.17.18 , CPT ) is an enzyme . (wikipedia.org)
  • Zinc D-Ala-D-Ala carboxypeptidase (EC 3.4.17.14, Zn2+ G peptidase, D-alanyl-D-alanine hydrolase, D-alanyl-D-alanine-cleaving carboxypeptidase, DD-carboxypeptidase, G enzyme, DD-carboxypeptidase-transpeptidase) is an enzyme. (wikipedia.org)
  • Enzyme activity was highly sensitive to inhibition by 1-(D-3-mercapto-2-methylpropanoyl)-L-proline (SQ 14225), a potent inhibitor of mammalian dipeptidyl carboxypeptidase (angiotensin-converting enzyme, peptidyl dipeptidase, EC 3.4.15.1). (pnas.org)
  • The "go or grow" poten-tial of gliomas is linked to the neuropeptide processing enzyme carboxypeptidase E and mediated by metabolic stress. (thefreedictionary.com)
  • With a New York University Cancer Institute colleague, the researchers reported that the mixture of free-floating blood proteins created by the enzyme carboxypeptidase N accurately predicted the presence of early-stage breast cancer tissue in mice and in a small population of human patients. (thefreedictionary.com)
  • Researchers from the Houston Methodist Research Institute and New York University Cancer Institute, conducted experiments on mice models and breast cancer patients, and found that a mixture of free-floating blood proteins created by carboxypeptidase N or CPN (an enzyme that plays a major role in modifying proteins after they are being created), accurately signalled the early stages of the deadly disease. (thefreedictionary.com)
  • PCR detection of the insertion/ deletion polymorphism of the human angiotensin converting enzyme gene (DCP1) (dipeptidyl carboxypeptidase 1). (thefreedictionary.com)
  • Members of the carboxypeptidase A family are synthesised as inactive molecules with propeptides that must be cleaved to activate the enzyme. (ebi.ac.uk)
  • Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity. (ebi.ac.uk)
  • A high-resolution carboxypeptidase-Zn 2+ -citrate complex was studied by X-ray diffraction and enzyme kinetics for the first time. (hindawi.com)
  • The citrate molecule acts as a competitive inhibitor of this benchmark zinc-dependent peptidase, chelating the catalytic zinc ion in the active site of the enzyme and inducing a conformational change such that carboxypeptidase adopts the conformation expected to occur by substrate binding. (hindawi.com)
  • Production of MTX from MTX-Phe, catalyzed by bovine pancreas carboxypeptidase A (CPA), was 250-fold faster than the corresponding reaction involving methotrexate-α-alanine, previously the best MTX peptide substrate for the enzyme. (aacrjournals.org)
  • A carboxypeptidase B-like enzyme was detected in the soluble fraction of purified insulin secretory granules, and implicated in insulin biosynthesis. (portlandpress.com)
  • Human CPN (carboxypeptidase N) is a tetrameric plasma enzyme containing two glycosylated 83 kDa non-catalytic/regulatory subunits that carry and protect two active catalytic subunits. (biochemj.org)
  • Reduced expression of carboxypeptidase E (CPE), a neuropeptide-processing enzyme, in a cell death-resistant glioma cell line and lower CPE expression levels in the cohort of GBM samples of The Cancer Genome Atlas compared to normal brain control specimens prompted us to analyze the function of CPE as a putative tumor suppressor gene. (biomedsearch.com)
  • The D-alanyl-d-alanine carboxypeptidase enzyme is essential for virulence in the Schu S4 strain of Francisella tularensis and a dacD mutant is able to provide protection against a pneumonic challenge. (bioportfolio.com)
  • The enzyme L,D-carboxypeptidase A is involved in the recycling of bacterial peptidoglycan and is essential in Escherichia coli during stationary phase. (synbiosis.com)
  • Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. (creative-enzymes.com)
  • Glutamate carboxypeptidase II (GCPII) is an enzyme encoded by the FOLH1 (folate hydrolase 1) gene. (reportsnreports.com)
  • There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. (polstate.com)
  • Most scientists in the field now refer to this enzyme as CPA1 , and to a related pancreatic carboxypeptidase as CPA2 . (chemeurope.com)
  • The NH2-terminal amino acid sequence was determined and turned out to be identical to the NH2-terminal sequence of the membrane-bound carboxypeptidase M. By precipitation with antibodies MAX.1 and MAX.11, membrane preparations of macrophages and placental microvilli were almost completely depleted of enzyme activity, indicating that the two antibodies indeed recognize carboxypeptidase M. Immunoreactivity of both antibodies correlates with the reported tissue distribution of enzyme activity. (uni-regensburg.de)
  • Carboxypeptidase E is a peptide processing enzyme, involved in cleaving numerous peptide precursors, including neuropeptides and hormones involved in appetite control and glucose metabolism. (ox.ac.uk)
  • Probable serine carboxypeptidase CPVL is an enzyme that in humans is encoded by the CPVL gene. (wikipedia.org)
  • Besides those macrophages-rich tissues, the heart and kidney also express high levels of CPVL mRNA.The enzyme is similar to the carboxypeptidases CATHA and SCPEP1, but no direct confirmation of the enzymatic activity was obtained so far. (wikipedia.org)
  • Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the biosynthesis of enkephalin in bovine adrenal chromaffin granules 1 . (elsevier.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Carboxypeptidase A4 (CPA4) in serum, plasma, tissue homogenates and other biological fluids. (noveoninc.com)
  • Carboxypeptidase is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of aprotein or peptide. (medchemexpress.com)
  • A collaborative international project involving researchers from the CEA (French Atomic Energy Commission), the CNRS (National Centre for Scientific Research), the Inserm (French National Institute of Health and Medical Research), the University of Grenoble-Alps, the University of Montpellier and the University of Stanford [1] has identified an enzyme, Tubulin CarboxyPeptidase (TCP), which is responsible for the biochemical transformation of cellular microtubules, or detyrosination. (cea.fr)
  • We offer Carboxypeptidase M Peptides and Carboxypeptidase M Proteins for use in common research applications: Blocking/Neutralizing, Control, ELISA, Protein Array, Western Blot. (novusbio.com)
  • Each Carboxypeptidase M Peptide and Carboxypeptidase M Protein is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. (novusbio.com)
  • The protein encoded by CPA6 belongs to the family of carboxypeptidases, which catalyze the release of C-terminal amino acid, and have functions ranging from digestion of food to selective biosynthesis of neuroendocrine peptides. (antikoerper-online.de)
  • We show here that the Caenorhabditis elegans egl-21 gene encodes a protein that is very similar to carboxypeptidase E (CPE) and is broadly expressed in the nervous system. (jneurosci.org)
  • Jager M, Lee MJ, Li C, Farmer SR, Fried SK, Layne MD. Aortic carboxypeptidase-like protein enhances adipose tissue stromal progenitor differentiation into myofibroblasts and is upregulated in fibrotic white adipose tissue. (harvard.edu)
  • The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. (genetex.com)
  • PGCP was co-purified from human placenta with lysosomal carboxypeptidase, cathepsin A, lysosomal endopeptidase, cathepsin D, and a gamma-interferon-inducible protein, IP-30, using an affinity chromatography on a Phe-Leu-agarose column. (sigmaaldrich.com)
  • Recombinant Rat Carboxypeptidase-B is a 35.1 kDa protein consisting of 307 amino acids. (biovendor.com)
  • Analysis of the purified carboxypeptidase by SDS/polyacrylamide-gel electrophoresis under either reducing or non-reducing conditions showed it to be a monomeric protein of apparent Mr 55,000. (portlandpress.com)
  • In this study, the regulation of aortic carboxypeptidase-like protein (ACLP) expression in VSMCs was investigated. (ahajournals.org)
  • Carboxypeptidase B (EC 3.4.17.2), also well known as protaminase, pancreatic procarboxy-peptidase B (PCPB), tissue carboxypeptidase B, peptidyl-L-lysine (L-arginine) hydrolaseis a highly pancreas-specific protein (PASP), and has been identified previously as a serum marker for acute pancreatitis and pancreatic graft rejection. (creative-enzymes.com)
  • Carboxypeptidase B2, also known as Carboxypeptidase U, Thrombin-activable fibrinolysis inhibitor, Plasma carboxypeptidase B, CPB2, is a secreted protein which belongs to the peptidase M14 family. (creativebiomart.net)
  • Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC 3.4.17.21) - Glutamate carboxypeptidase II (GCPII) is a membrane-bound binuclear zinc metallopeptidase with the highly expressed in nervous and prostatic tissue. (reportsnreports.com)
  • Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC 3.4.17.21) pipeline Target constitutes close to 9 molecules. (reportsnreports.com)
  • The latest report Glutamate Carboxypeptidase 2 - Pipeline Review, H2 2017, outlays comprehensive information on the Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC 3.4.17.21) targeted therapeutics, complete with analysis by indications, stage of development, mechanism of action (MoA), route of administration (RoA) and molecule type. (reportsnreports.com)
  • It also reviews key players involved in Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC 3.4.17.21) targeted therapeutics development with respective active and dormant or discontinued projects. (reportsnreports.com)
  • Recombinant trypsin,recombinant carboxypeptidase B and recombinant protein A won the Shanghai high-tech achievement transformation project in Sep.2013. (polstate.com)
  • Our laboratory has identified a secreted matrix protein, aortic carboxypeptidase-like protein (ACLP), which is upregulated in idiopathic pulmonary fibrosis. (bu.edu)
  • Recommended name: Cytosolic carboxypeptidase-like protein 5 EC= 3.4.17. (cusabio.com)
  • Humans, animals, and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. (medchemexpress.com)
  • Aspartic protease, [beta]-galactosidase, peroxidase and serine carboxypeptidase were detected in three Ephedra species. (thefreedictionary.com)
  • The Arabidopsis ( Arabidopsis thaliana ) genome encodes 51 proteins annotated as serine carboxypeptidase-like (SCPL) enzymes. (plantphysiol.org)
  • Carbonell, Juan 2004-10-17 00:00:00 A cDNA clone encoding a serine carboxypeptidase (PsCP), isolated from young fruits of Pisum sativum L., was used to study the temporal and spatial expression and hormonal regulation of serine carboxypeptidase during reproductive and vegetative development. (deepdyve.com)
  • This is the first report of a serine carboxypeptidase-like gene induced by gibberellins in reproductive and vegetative developing tissues in dicotyledoneous plants. (deepdyve.com)
  • The designation of CPVL is a true serine carboxypeptidase. (wikipedia.org)
  • Although the primary sequence displays the expected serine carboxypeptidase active site, the enzymatic activity remains to be demonstrated. (wikipedia.org)
  • Although the primary sequence of CPVL bears every hallmarks of a serine carboxypeptidase, the enzymatic function of CPVL has not been confirmed. (wikipedia.org)
  • This antibody has been assayed against 1.0µg of Carboxypeptidase Y in a standard capture ELISA using Peroxidase conjugated streptavidin and ABTS (2,2'-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid]) as a substrate for 30 minutes at RT. (abcam.com)
  • The following antibody was used in this experiment: Carboxypeptidase A1 Polyclonal Antibody from Thermo Fisher Scientific, catalog # PA5-39610, RRID AB_2556162. (thermofisher.com)
  • Carboxypeptidase M Polyclonal antibody specifically detects Carboxypeptidase M in Human samples. (fishersci.com)
  • Carboxypeptidase B2/CPB2 Polyclonal antibody specifically detects Carboxypeptidase B2/CPB2 in Human samples. (fishersci.com)
  • The following antibody was used in this experiment: Carboxypeptidase M Monoclonal Antibody (OTI1F8) from Thermo Fisher Scientific, catalog # MA5-26858, RRID AB_2722917. (thermofisher.com)
  • Carboxypeptidase B antibody LS-C713312 is an HRP-conjugated rabbit polyclonal antibody to Carboxypeptidase B (CPB) from human, mouse and rat. (lsbio.com)
  • Carboxypeptidase B antibody LS-C503531 is an AP-conjugated rabbit polyclonal antibody to human Carboxypeptidase B (CPB). (lsbio.com)
  • Immunoperoxidase staining of human pancreas with Rabbit anti Bovine carboxypeptidase A1 antibody ( AHP2054 ) and HISTAR detection kit . (bio-rad-antibodies.com)
  • Rabbit anti Bovine Carboxypeptidase A1 antibody used for the evaluation of carboxypepridase and pro-carboxypeptidase in mouse tissue lysates by western blotting. (bio-rad-antibodies.com)
  • Antigens Carboxypeptidase A2_CPA2 antibody storage GENTAUR recommends for long therm storage to freeze at -24 C. For short time storage up to 30 days we suggest fridge storage at 1 to 10 C. Prevent multiple freeze taw cycles of Antigens Carboxypeptidase A2_CPA2. (antibody-antibodies.com)
  • Potent inhibitor of pancreatic carboxypeptidase A with a Ki of 27 nM, and of the serine proteases trypsin, chymotrypsin and pancreatic elastase, with Ki values of 6.9 nM, 1.83 nM and 4 nM, respectively. (rcsb.org)
  • 1998). Among the studied inhibitors, only two are specific for MCP, i.e. , the potato carboxypeptidase inhibitor (PCI) and its close homolog found in tomato plants (TCI). (bio-protocol.org)
  • Enhanced Co 2+ activation and inhibitor binding of carboxypeptidase M at low pH. (portlandpress.com)
  • Carboxypeptidase G2 (CPG2) Inhibitor is a novel Carboxypeptidase G2 (CPG2) Inhibitor, Antitumor agents. (adooq.com)
  • ZJ 43 is a potent inhibitor of PSM and PSMAL (glutamate carboxypeptidase II and III). (adooq.com)
  • 2-MPPA is a selective glutamate carboxypeptidase II (GCP-II) inhibitor used in the treatment of neurological disorders associated with excessive activation of glutamatergic systems. (adooq.com)
  • The inhibitor appeared to cause lysis of E. coli during stationary phase, behavior that is similar to a previously described deletion mutant of L,D-carboxypeptidase A (M. F. Templin, A. Ursinus, and J.-V. Holtje, EMBO J. 18:4108-4117, 1999). (synbiosis.com)
  • CPR (identical to carboxypeptidase U [CPU], plasma carboxypeptidase B [plasma CPB]) has also been described as an inhibitor of fibrinolysis, and termed TAFI (thrombin activatable fibrinolysis inhibitor). (biomedcentral.com)
  • 2-PMPA is a potent and selective inhibitor of glutamate carboxypeptidase II ( GCPII ) with an IC 50 of 300 pM. (medchemexpress.com)
  • CPA inhibitor is a potent inhibitor for carboxypeptidase A (CPA). (medchemexpress.com)
  • Prostate-Specific Membrane Antigen (PSMA) is a transmembrane glutamate carboxypeptidase expressed on tumor-associated vasculature that positively regulates angiogenesis in a laminin-dependent manner. (thefreedictionary.com)
  • Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. (thefreedictionary.com)
  • A high-resolution structure of ligand-free human glutamate carboxypeptidase II. (nih.gov)
  • 11CMCG: Synthesis, uptake selectivity, and primate PET of a probe for glutamate carboxypeptidase II (NAALADase). (thefreedictionary.com)
  • Purification, cDNA cloning, and expression of a new human blood plasma glutamate carboxypeptidase homologous to N-acetyl-aspartyl-alpha-glutamate carboxypeptidase/prostate-specific membrane antigen. (sigmaaldrich.com)
  • We describe the identification, cDNA cloning, and biochemical characterization of a new human blood plasma glutamate carboxypeptidase (PGCP). (sigmaaldrich.com)
  • PGCP showed significant amino acid sequence homology to several cocatalytic metallopeptidases including a glutamate carboxypeptidase II also known as N-acetyl-aspartyl-alpha-glutamate carboxypeptidase or as prostate-specific membrane antigen and expressed glutamate carboxypeptidase activity. (sigmaaldrich.com)
  • Inhibition of glutamate carboxypeptidase II (GCPII) has been shown to be neuroprotective in multiple preclinical models in which dysregulated glutamatergic transmission is implicated. (elsevier.com)
  • A series of hydroxamic acids has been prepared as potential inhibitors of glutamate carboxypeptidase II (GCP II). (elsevier.com)
  • Here we report a novel mechanism by which secreted plasma glutamate carboxypeptidase(PGCP) negatively involves Wnt/β-catenin signaling by DKK4 regulation in liver cancer metastasis. (oncotarget.com)
  • Glutamate carboxypeptidase II (GCPII) is a membrane-bound binuclear zinc metallopeptidase with the highest expression levels found in the nervous and prostatic tissue. (eurekaselect.com)
  • C. Barinka, C. Rojas, B. Slusher and M. Pomper, " Glutamate Carboxypeptidase II in Diagnosis and Treatment of Neurologic Disorders and Prostate Cancer", Current Medicinal Chemistry (2012) 19: 856. (eurekaselect.com)
  • The ability of plasma carboxypeptidase B (pCPB) to remove these residues suggests that it may act as a suppressor of these Plg functions. (jci.org)
  • SNP detection of carboxypeptidase E gene and its association with meat quality and carcass traits in Korean cattle. (thefreedictionary.com)
  • This gene is a member of the carboxypeptidase A/B subfamily, and it is located in a cluster with three other family members on chromosome 7. (nih.gov)
  • The predicted amino-acid sequence of the cDNA clone contains the partially determined sequences of CPE, several pairs of basic amino acids and displays some homology with both carboxypeptidases A and B. Restriction analysis of bovine genomic DNA suggests only one gene for CPE. (elsevier.com)
  • Expression of carboxypeptidase M on mRNA level and enzymatic activity markedly increase during in vitro differentiation of monocytes, according to the described increase in MAX.1 and MAX.11 antigen expression. (uni-regensburg.de)
  • Two independent mutants of Escherichia coli deficient in dipeptidyl carboxypeptidase activity (Dep-) were isolated after mutagenesis with ethyl methanesulfonate. (pnas.org)
  • Ghosh AS, Chowdhury C, Nelson DE (2008) Physiological functions of D-alanine carboxypeptidases in Escherichia coli . (springer.com)
  • Chowdhury C, Nayak TR, Young KD et al (2010) A weak DD-carboxypeptidase activity explains the inability of PBP 6 to substitute for PBP 5 in maintaining normal cell shape in Escherichia coli . (springer.com)
  • The distribution of PBP5, the major D,D-carboxypeptidase in Escherichia coli, was mapped by immunolabelling and by visualization of GFP fusion proteins in wild-type cells and in mutants lacking one or more D,D-carboxypeptidases. (nih.gov)
  • Similar to that of carboxypeptidase A EC 3.4.17.1 , but with a preference for bulkier C-terminal residues. (rcsb.org)
  • carboxypeptidase A removes aromatic or branched hydrocarbons, while carboxypeptidase B removes positively charged terminal lysine or arginine amino acid residues. (thefreedictionary.com)
  • Proprotein convertases (PCs) cleave precursors after dibasic residues, and carboxypeptidases remove basic residues from the C terminals. (jneurosci.org)
  • Two critical processing steps are proteolytic cleavage after dibasic residues by proprotein convertases (PCs) and removal of the dibasic residues from the C terminals of the cleaved peptides by carboxypeptidases. (jneurosci.org)
  • Carboxypeptidase-E (CPE ) is a carboxypeptidase that cleaves C-terminal amino acid residues and is involved in the biosynthesis of peptide hormones and neurotransmitters. (prospecbio.com)
  • Carboxypeptidase-B sequentially cleaves C-terminal K and R residues. (biovendor.com)
  • Carboxypeptidases (CP), carboxypeptidase N (CPN) and carboxypeptidase R (CPR), have been reported as a protease, which can cleave carboxy-terminal arginine or lysine residues from biologically active peptides, such as C3a and C5a, and regulate their activity. (biomedcentral.com)
  • Carboxypeptidase A usually refers to the pancreatic exopeptidase which hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side chains. (chemeurope.com)
  • Background Removal of C-terminal lysine residues that are continuously exposed in lysing fibrin is an established anti-fibrinolytic mechanism dependent on the plasma carboxypeptidase TAFIa, which also removes arginines that are exposed at the time of fibrinogen clotting by thrombin. (elsevier.com)
  • Carboxypeptidases are proteases that hydrolyze the peptide bonds at the carboxy-terminal end of a chain of amino acids and have been identified in a wide variety of cell types and animals. (google.com)
  • Activation peptide of carboxypeptidase B and anionic trypsinogen as early predictors of the severity of acute pancreatitis. (thefreedictionary.com)
  • Methotrexate-α-phenylalanine (MTX-Phe), a second-generation prodrug in the MTX α-peptide series designed for activation to MTX by carboxypeptidase-mAb conjugates, was synthesized by reaction of the p -nitrophenyl ester of 4-amino-4-deoxy-10-methylpteroic acid with l -glutamyl-α- l -phenylalanine. (aacrjournals.org)
  • Recommend recombinant carboxypeptidase B lyophilized should be stored under 2-8℃ in sealed container. (polstate.com)
  • Stability:A sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage. (polstate.com)
  • Plasma levels of carboxypeptidase U (CPU, CPB2 or TAFIa) are elevated in patients with acute myocardial infarction. (nih.gov)
  • In addition to providing information about the specific role of this exopeptidase in E. coli, the Dep- mutants may prove useful for delineating the regulation and cellular function of dipeptidyl carboxypeptidases in higher organisms. (pnas.org)
  • CPA (carboxypeptidase A) is another MC protease, co-localized with chymase in severe atherosclerotic lesions. (portlandpress.com)
  • Vancomycin and ristocetin are shown to inhibit the hydrolysis of sensitive peptides by the Streptomyces albus G D-alanyl-D carboxypeptidase and the mechanism of inhibition is discussed. (ac.be)
  • Objective To evaluate the impact of alterations in fibrin structure mediated by constitutive carboxypeptidase activity on the function of fibrin as a template for tissue plasminogen activator-(tPA) induced plasminogen activation and its susceptibility to digestion by plasmin. (elsevier.com)
  • Sun L, Guo C, Burnett J, Pan J, Yang Z, Ran Y, Sun D. Association between expression of Carboxypeptidase 4 and stem cell markers and their clinical significance in liver cancer development. (jcancer.org)
  • This study aimed to evaluate the expression of carboxypeptidase 4 (CPA4) in hepatitis, liver cirrhosis and liver cancer tissues, and revealed its clinical significance in liver cancer progression. (jcancer.org)
  • Cloning and sequence analysis of cDNA for bovine carboxypeptidase E . Nature , 323 (6087), 461-464. (elsevier.com)
  • Fricker LD , Evans CJ, Esch FS, Herbert E. Cloning and sequence analysis of cDNA for bovine carboxypeptidase E . Nature . (elsevier.com)
  • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. (semanticscholar.org)
  • Within the secretory granules, carboxypeptidase E (CPE) activity is found in both a soluble and a membrane-bound form 1 , which differ slightly in relative molecular mass (M r ) 5 . (elsevier.com)
  • Within the secretory granules, carboxypeptidase E (CPE) activity is found in both a soluble and a membrane-bound form1, which differ slightly in relative molecular mass (Mr)5. (elsevier.com)
  • The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G". Eur. (wikipedia.org)
  • Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. (abcam.com)
  • amino acids with similar specificity as observed for the human pancreatic juice, whereas bovine carboxypeptidase B cleaved the basic amino acid conjugates. (eurekamag.com)
  • These experiments indicate that glycine and taurine amidates of cholic acid differ from a number of other conjugates with neutral and basic amino acid in being resistant to hydrolysis by pancreatic and plasma carboxypeptidases. (eurekamag.com)
  • YaxinBio is specialized in the research and the production of Animal Origin Free recombinant carboxypeptidase B and recombinant trypsin, which are of high importance for the production of human recombinant insulin. (thefreedictionary.com)
  • Carboxypeptidase A2 ( CPA2 ) is a secreted pancreatic procarboxy -peptidase, and cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. (sinobiological.com)
  • The fact that two of the least related proteins within this clade are acyltransferases rather than true serine carboxypeptidases suggests that some or all of the remaining members of this group may have similar activities. (plantphysiol.org)
  • Your search returned 53 carboxypeptidase A4 ELISA ELISA Kit across 8 suppliers. (biocompare.com)
  • Your search returned 24 carboxypeptidase, vitellogenic like ELISA ELISA Kit across 3 suppliers. (biocompare.com)
  • NOS1AP regulates dendrite patterning of hippocampal neurons through a carboxypeptidase E-mediated pathway. (nih.gov)
  • Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function. (harvard.edu)
  • Thrombin-activatable carboxypeptidase B cleavage of osteopontin regulates neutrophil survival and synoviocyte binding in rheumatoid arthritis. (semanticscholar.org)
  • Carboxypeptidases are zinc-containing exopeptidases that catalyze the release of carboxy-terminal amino acids, and are synthesized as zymogens that are activated by proteolytic cleavage. (nih.gov)
  • PBPs are also involved in PG remodeling by catalyzing DD-carboxypeptidase (DD-CPase) and endopeptidase reactions. (springer.com)

Xaa = any amino acid residue
↓ = cleavage site
P6P5P4P3P2P1P1′
XaaXaaXaaXaaXaaXaanot Ser