Carboxypeptidase U: 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.Carboxypeptidases: Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.Carboxypeptidase H: 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.Carboxypeptidase B: 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 A: 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.Lysine Carboxypeptidase: 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.Cathepsin A: 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.Glutamate Carboxypeptidase II: 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.gamma-Glutamyl Hydrolase: Catalyzes the hydrolysis of pteroylpolyglutamic acids in gamma linkage to pterolylmonoglutamic acid and free glutamic acid. EC 3.4.19.9.Amino Acid Sequence: 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.Molecular Sequence Data: 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.Muramoylpentapeptide Carboxypeptidase: Enzyme which catalyzes the peptide cross-linking of nascent CELL WALL; PEPTIDOGLYCAN.Serine-Type D-Ala-D-Ala Carboxypeptidase: 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.Vacuoles: Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion.Kinetics: The rate dynamics in chemical or physical systems.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Dipeptides: Peptides composed of two amino acid units.Penicillin G: 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.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Hydrogen-Ion Concentration: 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)GPI-Linked Proteins: A subclass of lipid-linked proteins that contain a GLYCOSYLPHOSPHATIDYLINOSITOL LINKAGE which holds them to the CELL MEMBRANE.Anaphylatoxins: 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.Saccharomyces cerevisiae: 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.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Zinc: 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.3-Mercaptopropionic Acid: An inhibitor of glutamate decarboxylase. It decreases the GAMMA-AMINOBUTYRIC ACID concentration in the brain, thereby causing convulsions.Trypsin: 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.Amino Acids: 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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Pancreas: 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.Molecular Weight: The sum of the weight of all the atoms in a molecule.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Cloning, Molecular: 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.Benzyl CompoundsBase Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Saccharomyces cerevisiae Proteins: 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.Chymases: 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.Protein Conformation: 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).Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Peptides: 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.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Aspergillus oryzae: 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.Ribonucleoprotein, U1 Small Nuclear: 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.Protein Processing, Post-Translational: 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.Peptidyl-Dipeptidase A: 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.Cattle: 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.Enzyme Stability: 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.Fibrinolysis: The natural enzymatic dissolution of FIBRIN.Blood Coagulation: The process of the interaction of BLOOD COAGULATION FACTORS that results in an insoluble FIBRIN clot.Hemostasis: The process which spontaneously arrests the flow of BLOOD from vessels carrying blood under pressure. It is accomplished by contraction of the vessels, adhesion and aggregation of formed blood elements (eg. ERYTHROCYTE AGGREGATION), and the process of BLOOD COAGULATION.Thrombin: An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN.Thrombomodulin: A cell surface glycoprotein of endothelial cells that binds thrombin and serves as a cofactor in the activation of protein C and its regulation of blood coagulation.

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)

*Carboxypeptidase

... 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 ...

*Carboxypeptidase A

... the zinc ion and assisted by residue Glu-270 Carboxypeptidase A inhibitor Carboxypeptidase B Carboxypeptidase Carboxypeptidase ... "Carboxypeptidase A" Acc. Chem. Res. (1989) 22: 62-69 Christianson, David et al. "Carboxypeptidase A" Acc. Chem. Res. (1989) 22 ... This property of carboxypeptidase A led to the first clause of Daniel E. Koshland, Jr.'s "induced fit" hypothesis. Several ... Carboxypeptidase A usually refers to the pancreatic exopeptidase that hydrolyzes peptide bonds of C-terminal residues with ...

*Carboxypeptidase B

... (EC 3.4.17.2, protaminase, pancreatic carboxypeptidase B, tissue carboxypeptidase B, peptidyl-L-lysine [L- ... Wallace, E.F.; Evans, C.J.; Jurik, S.M.; Mefford, I.N.; Barchas, J.D. (1982). "Carboxypeptidase B activity from adrenal medulla ... The MEROPS online database for peptidases and their inhibitors: M14.003 Carboxypeptidase B at the US National Library of ... doi:10.1016/0076-6879(70)19036-7. Brodrick, J.W.; Geokas, M.C.; Largman, C. (1976). "Human carboxypeptidase B. II. Purification ...

*Carboxypeptidase A6

Carboxypeptidase A inhibitor Carboxypeptidase GRCh38: Ensembl release 89: ENSG00000165078 - Ensembl, May 2017 GRCm38: Ensembl ... Carboxypeptidase A6 (CPA6) is an metallocarboxypeptidase enzyme that in humans is encoded by the CPA6 gene. It is highly ... The protein encoded by this gene belongs to the family of carboxypeptidases, which catalyze the release of C-terminal amino ... Lyons, P. J.; Callaway, M. B.; Fricker, L. D. (2008). "Characterization of Carboxypeptidase A6, an Extracellular Matrix ...

*Carboxypeptidase D

... carboxypeptidase Kex1, gene KEX1 serine carboxypeptidase, KEX1 carboxypeptidase, KEX1 proteinase, KEX1DELTAp, CPDW-II, serine ... Carboxypeptidase D can refer to one of several enzymes. A family of serine carboxypeptidases (i.e. enzymes that use an active ... Song L, Fricker LD (1995). "Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, ... Carboxypeptidase D at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ...

*Carboxypeptidase C

... (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ... Carboxypeptidase C at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ... Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... deamidase, lysosomal carboxypeptidase A, phaseolin) is an enzyme. This enzyme catalyses the following chemical reaction Release ...

*Muramoyltetrapeptide carboxypeptidase

... 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 ...

*Carboxypeptidase B2

... (CPB2), also known as carboxypeptidase U (CPU), plasma carboxypeptidase B (pCPB) or thrombin-activatable ... 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 ( ... "Entrez Gene: CPB2 carboxypeptidase B2 (plasma)". Bouma BN, Mosnier LO (2005). "Thrombin activatable fibrinolysis inhibitor ( ...

*Lysine carboxypeptidase

... (EC 3.4.17.3, carboxypeptidase N, arginine carboxypeptidase, kininase I, anaphylatoxin inactivator, ... Lysine carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Plummer, T.H. Jr.; Erdös, E.G. (1981). "Human plasma carboxypeptidase N". Methods Enzymol. 80: 442-449. doi:10.1016/s0076-6879( ... Skidgel, R.A. (1988). "Basic carboxypeptidases: regulators of peptide hormone activity". Trends Pharmacol. Sci. 9: 301-303. doi ...

*Carboxypeptidase A2

"Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2 ... Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2 gene. Three different forms of human pancreatic ... "Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic)". Pascual R, Burgos FJ, Salva M, et al. (1989). "Purification and properties ...

*Carboxypeptidase A1

... is an enzyme that in humans is encoded by the CPA1 gene. Three different forms of human pancreatic ... Carboxypeptidase A1 is a monomeric pancreatic exopeptidase. It is involved in zymogen inhibition. GRCh38: Ensembl release 89: ... Stewart EA, Craik CS, Hake L, Bowcock AM (1990). "Human carboxypeptidase A identifies a BglII RFLP and maps to 7q31-qter". Am. ... 1986). "Assignment of the gene for carboxypeptidase A to human chromosome 7q22----qter and to mouse chromosome 6". Hum. Genet. ...

*Carboxypeptidase T

"Carboxypeptidase T - an extracellular carboxypeptidase of thermophilic actinomycetes - a remote analog of animal ... Carboxypeptidase T (EC 3.4.17.18, CPT) is an enzyme. This enzyme catalyses the following chemical reaction Releases a C- ... Carboxypeptidase T at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ... "Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris". Eur. J. Biochem. 208: 281-288. doi:10.1111/j.1432- ...

*Carboxypeptidase Taq

"Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1". ... Carboxypeptidase Taq (EC 3.4.17.19) is an enzyme. This enzyme catalyses the following chemical reaction Release of a C-terminal ... Carboxypeptidase Taq at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Lee, S.-H.; Taguchi, H.; Yoshimura, E.; Minagawa, E.; Kaminogawa, S.; Ohta, T.; Matsuzawa, H. (1994). "Carboxypeptidase Taq, a ...

*Carboxypeptidase M

... (EC 3.4.17.12, CPM) is an enzyme. This enzyme catalyses the following chemical reaction Cleavage of C- ... Carboxypeptidase M at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ... Deddish, P.A.; Skidgel, R.A.; Erdös, E.G. (1989). "Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low ... Skidgel, R.A.; Davis, R.M.; Tan, F. (1989). "Human carboxypeptidase M. Purification and characterization of membrane-bound ...

*Zinc carboxypeptidase

The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A ( ... "Primary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family". J. ... Structural studies of carboxypeptidases A and B reveal the propeptide to exist as a globular domain, followed by an extended ... Members of the carboxypeptidase A family are synthesised as inactive molecules with propeptides that must be cleaved to ...

*Alanine carboxypeptidase

... (EC 3.4.17.6, N-benzoyl-L-alanine-amidohydrolase) is an enzyme. This enzyme catalyses the following ... Alanine carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ...

*Muramoylpentapeptide carboxypeptidase

D-alanine carboxypeptidase I, DD-carboxypeptidase, D-alanine carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanine-D ... carboxypeptidase, carboxypeptidase D-alanyl-D-alanine, carboxypeptidase I, UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine ... Muramoylpentapeptide carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... Purification and properties of two D-alanine carboxypeptidases from Escherichia coli". J. Biol. Chem. 243: 3193-3201. PMID ...

*Carboxypeptidase U

... (EC 3.4.17.20, arginine carboxypeptidase, carboxypeptidase R, plasma carboxypeptidase B, thrombin- ... Wang, W.; Hendriks, D.F.; Scharpé, S. (1994). "Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen ... plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U. Carboxypeptidase Eaton, D.L ... Carboxypeptidase U at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ...

*Glutamate carboxypeptidase

... (EC 3.4.17.11, carboxypeptidase G, carboxypeptidase G1, carboxypeptidase G2, glutamyl ... Glutamate carboxypeptidase II Goldman, P.; Levy, C.C. (1967). "Carboxypeptidase G: purification and properties". Proc. Natl. ... Glutamate carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... McCullogh, J.L.; Chabner, B.A.; Bertino, J.R. (1971). "Purification and properties of carboxypeptidase G1". J. Biol. Chem. 246 ...

*Carboxypeptidase E

... (CPE), also known as carboxypeptidase H (CPH) and enkephalin convertase, is an enzyme that in humans is ... Carboxypeptidase Carboxypeptidase A GRCh38: Ensembl release 89: ENSG00000109472 - Ensembl, May 2017 GRCm38: Ensembl release 89 ... fills in for carboxypeptidase E in this organism. In humans, CPE is encoded by the CPE gene. Carboxypeptidase E functions in ... Carboxypeptidase E is not found in the fruit fly (Drosophila), and another enzyme (presumably carboxypeptidase D) ...

*DD-carboxypeptidase

... may refer to: Muramoylpentapeptide carboxypeptidase, an enzyme Zinc D-Ala-D-Ala carboxypeptidase, an enzyme ...

*Potato carboxypeptidase inhibitor

PCI also inhibits carboxypeptidase R without affecting the activity of carboxypeptidase N in the circulation and have therefore ... May 1998). "Potato carboxypeptidase inhibitor, a T-knot protein, is an epidermal growth factor antagonist that inhibits tumor ... Potato carboxypeptidase inhibitor (PCI) is a naturally occurring protease inhibitor peptide in potatoes that can form complexes ... a Redlitz A, Tan AK, Eaton DL, Plow EF (November 1995). "Plasma carboxypeptidases as regulators of the plasminogen system". J. ...

*Carboxypeptidase A inhibitor

The structure of the complex between bovine carboxypeptidase A and the 39-amino-acid carboxypeptidase A inhibitor from potatoes ... Hass GM, Nau H, Biemann K, Grahn DT, Ericsson LH, Neurath H (March 1975). "The amino acid sequence of a carboxypeptidase ... In molecular biology, the carboxypeptidase A inhibitor family is a family of proteins which is represented by the well- ... Rees DC, Lipscomb WN (August 1980). "Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-A resolution". Proc ...

*Glutamate carboxypeptidase II

... (GCPII), also known as N-acetyl-L-aspartyl-L-glutamate peptidase I (NAALADase I), NAAG peptidase ... All of which refer to the same protein glutamate carboxypeptidase II. GCPII is mainly expressed in four tissues of the body, ... and carboxypeptidase activity based on the parent tissue. The hydrolysis of NAAG by GCPII obeys Michaelis-Menten kinetics ...

*Gly-X carboxypeptidase

Gly-Xaa carboxypeptidase (EC 3.4.17.4, glycine carboxypeptidase, carboxypeptidase a, carboxypeptidase S, peptidase alpha, yeast ... Gly-Xaa carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Wolf, D.H.; Ehmann, C. (1978). "Carboxypeptidase S from yeast: regulation of its activity during vegetative growth and ... carboxypeptidase) is an enzyme. This enzyme catalyses the following chemical reaction Release of a C-terminal amino acid from a ...
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 ...
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 ...
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 1 - Detects Human Thrombin Activatable Fibrinolysis Inhibitor (TAFI) and activated TAFI. Mouse monoclonal of isotype IgG1.
Anti-Human TAFI Clone 3 - Detects Human Thrombin Activatable Fibrinolysis Inhibitor (TAFI) and activated TAFI. Mouse monoclonal of isotype IgG3.
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 ...
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) ...
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: ...
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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 ...
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 - 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 ...
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.
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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...
Prolonged use of reformulated and the original 2-rod Norplant® implants showed similar changes in most hemostatic parameters studied. Raised hemoglobin concentration and hematocrit values with no enhanced platelet activation or significant changes in platelet numbers were seen. Factor VII showed an increase from 18 months compared to the first 12 months of original Norplant implant use, while with reformulated Norplant implant, the level at 36 months was significantly higher than the first 24 months of implant use. Fibrinogen levels were significantly elevated by 36 months of both implant use. No evidence of enhanced activation of coagulation, fibrinolysis/inhibitor were observed during prolonged implant use. Overall, no significant changes in tissue plasminogen activator (t-PA) levels were observed but urokinase-like plasminogen activator (u-PA) levels were significantly reduced, indicating no enhancement of tissue breakdown. Plasminogen activator inhibitor (PAI-1) antigen levels were ...
As part of a large-scale study of menstrual blood loss in the community serum fibrin degradation products were measured soon after menstruation in 331 women. No significant correlation was found between the amount of blood lost and the serum level of fibrin degradation products. These findings conflict with reports suggesting that excessive intrauterine fibrinolysis, which may play a part in menorrhagia, is associated with raised serum F.D.P. concentrations.. ...
The following sample terms are included for reference. Expand at first mention in accordance with , Abbreviations, Clinical, Technical, and Other Common Terms. Note: Protein C was named for an investigators chromatographic fraction C in which it was discovered. The S in protein S refers to Seattle, where it was discovered. Protein S is not the same as S protein; see also , Complement. The following sample terms represent entities that take part in fibrinolysis or its inhibition. Expand at first mention in accordance with , Abbreviations, Clinical, Technical, and Other Common Terms: Two among several tests of coagulation are
Lysosomal Pro-X Carboxypeptidase/PRCP Overexpression Lysate (Denatured). Tested Reactivity: Hu. Validated: WB. Backed by our 100% Guarantee.

Zinc D-Ala-D-Ala carboxypeptidase - WikipediaZinc D-Ala-D-Ala carboxypeptidase - Wikipedia

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". ...
more infohttps://en.wikipedia.org/wiki/Zinc_D-Ala-D-Ala_carboxypeptidase

Characterization of the Mouse Aortic Carboxypeptidase-Like Protein Promoter Reveals Activity in Differentiated and...Characterization of the Mouse Aortic Carboxypeptidase-Like Protein Promoter Reveals Activity in Differentiated and...

... the carboxypeptidase-like domain of mouse ACLP is similar in structure to the rat carboxypeptidase E gene.39 It is possible ... Layne MD, Endege WO, Jain MJ, Yet S-F, Hsieh C-M, Chin MT, Perrella MA, Blanar MA, Haber E, Lee M-E. Aortic carboxypeptidase- ... Gomis-Rüth FX, Companys V, Qian Y, Fricker LD, Vendrell J, Avilés FX, Coll M. Crystal structure of avian carboxypeptidase D ... The discoidin-like domain is encoded by exons 11 through 14, whereas the carboxypeptidase-like domain of ACLP is generated by ...
more infohttp://circres.ahajournals.org/content/90/6/728.long

Carboxypeptidase B2Carboxypeptidase B2

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 ( ... Plasma levels of carboxypeptidase U (CPU, CPB2 or TAFIa) are elevated in patients with acute myocardial infarction.. ... Generation of a stable thrombin-activatable fibrinolysis inhibitor deletion mutant exerting full carboxypeptidase activity ...
more infohttps://pharos.nih.gov/idg/targets/Q96IY4

Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate...Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate...

Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane... ... Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth ... 38 Pages Report] Check for Discount on Glutamate Carboxypeptidase 2 ( ... Glutamate carboxypeptidase II (GCPII) is an enzyme encoded by the FOLH1 (folate hydrolase 1) gene. GCPII is intimately involved ...
more infohttp://www.reportsnreports.com/reports/1173537-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-341721-pi-w-h2-2017.html

Plasma glutamate carboxypeptidase is a negative regulator in liver cancer metastasis | OncotargetPlasma glutamate carboxypeptidase is a negative regulator in liver cancer metastasis | Oncotarget

Plasma glutamate carboxypeptidase is a negative regulator in liver cancer metastasis ... Suban D, Zajc T, Renko M, Turk B, Turk V, Dolenc I. Cathepsin C and plasma glutamate carboxypeptidase secreted from Fischer rat ... Plasma glutamate carboxypeptidase (PGCP) is a secreted protein hydrolyzing the circulating peptides in the extracellular ... Here we report a novel mechanism by which secreted plasma glutamate carboxypeptidase(PGCP) negatively involves Wnt/β-catenin ...
more infohttp://www.oncotarget.com/index.php?journal=oncotarget&page=article&op=view&path%5B%5D=12967&path%5B%5D=41081

Ambivalent roles of carboxypeptidase B in the lytic susceptibility of fibrin<...Ambivalent roles of carboxypeptidase B in the lytic susceptibility of fibrin<...

Ambivalent roles of carboxypeptidase B in the lytic susceptibility of fibrin. Thrombosis research. 2014 Jan 1;133(1):80-87. ... Ambivalent roles of carboxypeptidase B in the lytic susceptibility of fibrin. In: Thrombosis research. 2014 ; Vol. 133, No. 1. ... keywords = "Carboxypeptidase, Fibrin, Fibrinolysis, Plasmin, tPA",. author = "Andr{\a}s Kov{\a}cs and L{\a}szl{\o} Szab{\o ... Ambivalent roles of carboxypeptidase B in the lytic susceptibility of fibrin. András Kovács, László Szabó, Colin Longstaff, ...
more infohttps://hungary.pure.elsevier.com/en/publications/ambivalent-roles-of-carboxypeptidase-b-in-the-lytic-susceptibilit

Cloning and sequence analysis of cDNA for bovine carboxypeptidase E<...Cloning and sequence analysis of cDNA for bovine carboxypeptidase E<...

N2 - Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the ... AB - Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the ... Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the ... abstract = "Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in ...
more infohttps://einstein.pure.elsevier.com/en/publications/cloning-and-sequence-analysis-of-cdna-for-bovine-carboxypeptidase-2

Glutamate Carboxypeptidase II - New β-secretase inhibitors for treatment of Alzheimers diseaseGlutamate Carboxypeptidase II - New β-secretase inhibitors for treatment of Alzheimer's disease

Glutamate Carboxypeptidase II. Published January 11, 2019. Background. MIC. Nevertheless, MARS identified harmful connections ...
more infohttp://healthyguide.info/category/glutamate-carboxypeptidase-ii/

Glutamate Carboxypeptidase IIGlutamate Carboxypeptidase II

Category: Glutamate Carboxypeptidase II. The manuscript addresses an extremely intriguing question of reason behind recurrent. ... Posted in Glutamate Carboxypeptidase IITagged Amyloid b-Peptide (1-42) human biological activity, Rabbit Polyclonal to OR52E2 ... Posted in Glutamate Carboxypeptidase IITagged Gpc4, Obatoclax mesylate inhibitor Posts navigation. ← Older posts ... Posted in Glutamate Carboxypeptidase IITagged buy Limonin, IFITM2 Ionic liquid based, microwave-assisted extraction (ILMAE) was ...
more infohttp://www.ecologicalsgardens.com/category/glutamate-carboxypeptidase-ii/

Structure of the carboxypeptidase B complex with N-sulfamoyl-L-phenylalanine - a transition state analog of non-specific...Structure of the carboxypeptidase B complex with N-sulfamoyl-L-phenylalanine - a transition state analog of non-specific...

Аннотация: Carboxypeptidase B (EC 3.4.17.2) (CPB) is commonly used in the industrial insulin production and as a template for ... Carboxypeptidase B (EC 3.4.17.2) (CPB) is commonly used in the industrial insulin production and as a template for drug design ... Structure of the carboxypeptidase B complex with N-sulfamoyl-L-phenylalanine - a transition state analog of non-specific ... Structure of the carboxypeptidase b complex with n-sulfamoyl-l-phenylalanine - a transition state analog of non-specific ...
more infohttps://istina.msu.ru/publications/article/60647856/

Carboxypeptidase E (CPE) is a prohormone/proneuropeptide handling enzyme and mice bearing - How NF-B is activated: the role of...Carboxypeptidase E (CPE) is a prohormone/proneuropeptide handling enzyme and mice bearing - How NF-B is activated: the role of...

Carboxypeptidase E (CPE) is a prohormone/proneuropeptide handling enzyme and mice bearing CPE mutations display an obese and ... carboxypeptidase E (CPE) is normally a digesting enzyme thats highly portrayed in endocrine cells and peptidergic neurons (17 ... By cancercurehere with Comments Off on Carboxypeptidase E (CPE) is a prohormone/proneuropeptide handling enzyme and mice ... Carboxypeptidase E (CPE) is a prohormone/proneuropeptide handling enzyme and mice bearing. ...
more infohttp://cancercurehere.com/?p=2070

Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. - Oxford...Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. - Oxford...

... polyglutamylated folates which are digested to monoglutamyl folates by the action of folylpoly-gamma-glutamate carboxypeptidase ... Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. ... Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. ... Aged, Alleles, Alternative Splicing, Animals, Antigens, Surface, COS Cells, Carboxypeptidases, Cloning, Molecular, DNA ...
more infohttps://www.ctsu.ox.ac.uk/publications/49324

Thrombin activatable fibrinolysis inhibitor and other hemostatic parameters in patients with essential arterial hypertension.Thrombin activatable fibrinolysis inhibitor and other hemostatic parameters in patients with essential arterial hypertension.

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. ...
more infohttp://www.biomedsearch.com/nih/Thrombin-activatable-fibrinolysis-inhibitor-other/18405171.html

IJMS  | Free Full-Text | Angiotensin-Converting Enzymes Play a Dominant Role  in Fertility | HTMLIJMS | Free Full-Text | Angiotensin-Converting Enzymes Play a Dominant Role in Fertility | HTML

Cloning and functional expression as a captopril-insensitive carboxypeptidase. J. Biol. Chem 2000, 275, 33238-33243. [Google ... The full-length human ACE2 cDNA predicts an endothelium-bound carboxypeptidase of 805 amino acids, which has 42% homology with ... A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ. Res 2000 ...
more infohttp://mdpi.com/1422-0067/14/10/21071/htm

Thrombin-Activatable Fibrinolysis Inhibitor | Bentham ScienceThrombin-Activatable Fibrinolysis Inhibitor | Bentham Science

Keywords:tafi, cpu, cpr, cpb, carboxypeptidase, coagulation, fibrinolysis. Abstract: The coagulation system is a potent ...
more infohttp://www.eurekaselect.com/62979/article/thrombin-activatable-fibrinolysis-inhibitor

Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: Localization to the trans-Golgi network and recycling...Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: Localization to the trans-Golgi network and recycling...

Carboxypeptidase D (CPD) is a recently discovered membrane-bound metallocarboxypeptidase that has been proposed to be involved ... N2 - Carboxypeptidase D (CPD) is a recently discovered membrane-bound metallocarboxypeptidase that has been proposed to be ... AB - Carboxypeptidase D (CPD) is a recently discovered membrane-bound metallocarboxypeptidase that has been proposed to be ... abstract = "Carboxypeptidase D (CPD) is a recently discovered membrane-bound metallocarboxypeptidase that has been proposed to ...
more infohttps://ohsu.pure.elsevier.com/en/publications/intracellular-trafficking-of-metallocarboxypeptidase-d-in-att-20--2

A novel PSMA/GCPII-deficient mouse model shows enlarged seminal vesicles upon agingA novel PSMA/GCPII-deficient mouse model shows enlarged seminal vesicles upon aging

... also known as glutamate carboxypeptidase II (GCPII), is an important diagnostic and therapeutic target in prostate cancer. PSMA ... Prostate-specific membrane antigen (PSMA), also known as glutamate carboxypeptidase II (GCPII), is an important diagnostic and ...
more infohttps://www.urotoday.com/recent-abstracts/urologic-oncology/prostate-cancer/107226-a-novel-psma-gcpii-deficient-mouse-model-shows-enlarged-seminal-vesicles-upon-aging.html

Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI) | BMC Biochemistry | Full TextBiochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI) | BMC Biochemistry | Full Text

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 ...
more infohttps://bmcbiochem.biomedcentral.com/articles/10.1186/1471-2091-10-13

Oalib searchOalib search

Glutamate carboxypeptidase II (GCPII) C1561T and cytosolic serine hydroxymethyl transferase (cSHMT) C1420T polymorphisms were ...
more infohttp://www.oalib.com/search?kw=Shree%20Divyya&searchField=authors

Carboxypeptidase T - WikipediaCarboxypeptidase T - Wikipedia

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- ...
more infohttps://en.wikipedia.org/wiki/Carboxypeptidase_T

Carboxypeptidase A definition | Drugs.comCarboxypeptidase A definition | Drugs.com

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 ...
more infohttps://www.drugs.com/dict/carboxypeptidase-a.html
  • 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)
  • 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)
  • 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)
  • 2017. Carboxypeptidase B (EC 3.4.17.2) (CPB) is commonly used in the industrial insulin production and as a template for drug design. (msu.ru)
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