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 22.214.171.124 and EC 126.96.36.199.
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.
Amino Acid Sequence
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.
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.
Sequence Homology, Amino Acid
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.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
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).
Cloning, expression, and substrate specificity of MeCPA, a zinc carboxypeptidase that is secreted into infected tissues by the fungal entomopathogen Metarhizium anisopliae. (1/264)To date zinc carboxypeptidases have only been found in animals and actinomycete bacteria. A cDNA clone (MeCPA) for a novel fungal (Metarhizium anisopliae) carboxypeptidase (MeCPA) was obtained by using reverse transcription differential display polymerase chain reaction to identify pathogenicity genes. MeCPA resembles pancreatic carboxypeptidases in being synthesized as a precursor species (418 amino acids) containing a large amino-terminal fragment (99 amino acids). The mature (secreted) form of MeCPA shows closest amino acid identity to human carboxypeptidases A1 (35%) and A2 (37%). MeCPA was expressed in an insect cell line yielding an enzyme with dual A1 + A2 specificity for branched aliphatic and aromatic COOH-terminal amino acids. However, in contrast to the very broad spectrum A + B-type bacterial enzymes, MeCPA lacks B-type activity against charged amino acids. This is predictable as key catalytic residues determining the specificity of MeCPA are conserved with those of mammalian A-type carboxypeptidases. Thus, in evolutionary terms the fungal enzyme is an intermediate between the divergence of A and B forms and the differentiation of the A form into A1 and A2 isoforms. Ultrastructural immunocytochemistry of infected host (Manduca sexta) cuticle demonstrated that MeCPA participates with the concurrently produced endoproteases in procuring nutrients; an equivalent function to digestive pancreatic enzymes. (+info)
Cloning, sequencing and functional expression of a cDNA encoding porcine pancreatic preprocarboxypeptidase A1. (2/264)A full-length cDNA clone coding for porcine pancreatic preprocarboxypeptidase A1 (prePCPA1) was isolated from a cDNA library. The open reading frame (ORF) of the nucleotide sequence was 1260 nt in length and encoded a protein of 419 amino acids (aa). The cDNA included a short signal peptide of 16 aa and a 94 aa-long activation segment. The calculated molecular mass of the mature proenzyme was 45561 Da, in accordance with that of the purified porcine pancreatic PCPA1. The deduced aa sequence of the corresponding enzyme differed from that predicted by the three-dimensional structure by 40 aa, and showed 85% identity and 55% identity to that of procarboxypeptidases A1 and A2, respectively. Moreover the sequence was identical to that of several independent cDNA clones, suggesting that it is the major transcribed gene. No evidence for a second variant was observed in the cDNA library and PCPA2 is apparently absent from the porcine pancreas. The cDNA was expressed in Saccharomyces cerevisiae under the control of the yeast triose phosphate isomerase promoter. The signal peptide of the PCPA protein efficiently directed its secretion into the culture medium (1.5 mg.L-1) as a protein of the predicted size. The recombinant proenzyme was analyzed by immunological and enzymological methods. Its activation behavior was comparable with that of the native form and led to a 35-kDa active enzyme. (+info)
Effect of self-association of alphas1-casein and its cleavage fractions alphas1-casein(136-196) and alphas1-casein(1-197),1 on aromatic circular dichroic spectra: comparison with predicted models. (3/264)The self-association of native alphas1-casein is driven by a sum of interactions which are both electrostatic and hydrophobic in nature. The dichroism of aromatic side chains was used to derive regio-specific evidence in relation to potential sites of alphas1-casein polymerization. Near-ultraviolet circular dichroism (CD) revealed that both tyrosine and tryptophan side chains play a role in alphas1-casein associations. Spectral evidence shows these side chains to be in an increasingly nonaqueous environment as both ionic strength and protein concentration lead to increases in the degree of self-association of the protein from dimer to higher oligomers. Near-UV CD investigation of the carboxypeptidase A treated peptide, alphas1-casein(1-197), indicated that the C-terminal residue (Trp199) may be superficial to these interactions, and that the region surrounding Trp164 is more directly involved in an aggregation site. Similar results for the cyanogen bromide cleavage peptide alphas1-casein(136-196) indicated the presence of strongly hydrophobic interactions. Association constants for the peptides of interest were determined by analytical ultracentrifugation, and also were approximated from changes in the near-UV CD curves with protein concentration. Sedimentation equilibrium experiments suggest the peptide to be dimeric at low ionic strength; like the parent protein, the peptide further polymerizes at elevated (0.224 M) ionic strength. The initial site of dimerization is suggested to be the tyrosine-rich area near Pro147, while the hydrophobic region around Pro168, containing Trp164, may be more significant in the formation of higher-order aggregates. (+info)
Carboxypeptidase A3 (CPA3): a novel gene highly induced by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells. (4/264)Butyrate and its structural analogues have recently entered clinical trials as a potential drug for differentiation therapy of advanced prostate cancer. To better understand the molecular mechanism(s) involved in prostate cancer differentiation, we used mRNA differential display to identify the gene(s) induced by butyrate. We found that the androgen-independent prostate cancer cell line PC-3 undergoes terminal differentiation and apoptosis after treatment with sodium butyrate (NaBu). A novel cDNA designated carboxypeptidase A3 (CPA3), which was up-regulated in NaBu-treated PC-3 cells, was identified and characterized. This gene expresses a 2795-bp mRNA encoding a protein with an open reading frame of 421 amino acids. CPA3 has 37-63% amino acid identity with zinc CPs from different mammalian species. It also shares 27-43% amino acid similarity with zinc CPs from several nonmammalian species, including Escherichia coli, yeast, Caenorhabditis elegans, and Drosophila. The structural similarity between CPA3 and its closest homologues indicates that the putative CPA3 protein contains a 16-residue signal peptide sequence, a 95-residue NH2-terminal activation segment, and a 310-residue CP enzyme domain. The consistent induction of CPA3 by NaBu in several prostate cancer cell lines led us to investigate the signaling pathway involved in the induction of CPA3 mRNA. Trichostatin A, a potent and specific inhibitor of histone deacetylase, also induced CPA3 mRNA expression, suggesting that CPA3 gene induction is mediated by histone hyperacetylation. We demonstrated that CPA3 induction was a downstream effect of the treatment with butyrate or trichostatin A, but that the induction of p21(WAF1/CIP1) occurred immediately after these treatments. We also demonstrated that the induction of CPA3 mRNA by NaBu was inhibited by p21(WAF1/CIP1) antisense mRNA expression, indicating that p21 transactivation is required for the induction of CPA3 by NaBu. Our data demonstrate that the histone hyperacetylation signaling pathway is activated during NaBu-mediated differentiation of PC-3 cells, and the new gene, CPA3, is involved in this pathway. (+info)
A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli. (5/264)The first gene of a family of prokaryotic proteases with a specificity for L,D-configured peptide bonds has been identified in Escherichia coli. The gene named ldcA encodes a cytoplasmic L, D-carboxypeptidase, which releases the terminal D-alanine from L-alanyl-D-glutamyl-meso-diaminopimelyl-D-alanine containing turnover products of the cell wall polymer murein. This reaction turned out to be essential for survival, since disruption of the gene results in bacteriolysis during the stationary growth phase. Owing to a defect in muropeptide recycling the unusual murein precursor uridine 5'-pyrophosphoryl N-acetylmuramyl-tetrapeptide accumulates in the mutant. The dramatic decrease observed in overall cross-linkage of the murein is explained by the increased incorporation of tetrapeptide precursors. They can only function as acceptors and not as donors in the crucial cross-linking reaction. It is concluded that murein recycling is a promising target for novel antibacterial agents. (+info)
Albumin banks peninsula: a new termination variant characterised by electrospray mass spectrometry. (6/264)Albumin Banks Peninsula is an electrophoretically fast variant that is expressed at only 2% of the total serum albumin. Electrospray ionisation analysis indicated a mass decrease of 755 Da relative to normal albumin and carboxypeptidase A digestion, together with CNBr peptide mapping, indicated a C-terminal truncation. This was confirmed by PCR and DNA sequence analysis which showed the introduction of a new AG acceptor splice site near the 3' end of intron 13. Predictably this results in the replacement of the C-terminal GKKLVAASQAALGL sequence by SLCSG and would be associated with an 861 Da decrease in molecular mass. We surmised that the new Cys was most probably cysteinylated as this albumin species would have a mass decrease of 742 Da and be very close to the measured value of 755 Da. Cysteinylation was confirmed when a mass decrease of 863 Da was measured between the proteins after reduction of their disulfide bonds. (+info)
Enhancement of heparin cofactor II anticoagulant activity. (7/264)Heparin cofactor II (HCII) is a serpin whose thrombin inhibition activity is accelerated by glycosaminoglycans. We describe the novel properties of a carboxyl-terminal histidine-tagged recombinant HCII (rHCII-CHis(6)). Thrombin inhibition by rHCII-CHis(6) was increased >2-fold at approximately 5 microgram/ml heparin compared with wild-type recombinant HCII (wt-rHCII) at 50-100 microgram/ml heparin. Enhanced activity of rHCII-CHis(6) was reversed by treatment with carboxypeptidase A. We assessed the role of the HCII acidic domain by constructing amino-terminal deletion mutants (Delta1-52, Delta1-68, and Delta1-75) in wt-rHCII and rHCII-CHis(6). Without glycosaminoglycan, unlike wt-rHCII deletion mutants, the rHCII-CHis(6) deletion mutants were less active compared with full-length rHCII-CHis(6). With glycosaminoglycans, Delta1-68 and Delta1-75 rHCIIs were all less active. We assessed the character of the tag by comparing rHCII-CHis(6), rHCII-CAla(6), and rHCII-CLys(6) to wt-rHCII. Only rHCII-CHis(6) had increased activity with heparin, whereas all three mutants have increased heparin binding. We generated a carboxyl-terminal histidine-tagged recombinant antithrombin III to study the tag on another serpin. Interestingly, this mutant antithrombin III had reduced heparin cofactor activity compared with wild-type protein. In a plasma-based assay, the glycosaminoglycan-dependent inhibition of thrombin by rHCII-CHis(6) was significantly greater compared with wt-rHCII. Thus, HCII variants with increased function, such as rHCII-CHis(6), may offer novel reagents for clinical application. (+info)
2'-carboxy-D-arabitinol 1-phosphate protects ribulose 1, 5-bisphosphate carboxylase/oxygenase against proteolytic breakdown. (8/264)Trypsin-catalysed cleavage of purified ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) and the resultant irreversible loss of carboxylase activity were prevented by prior incubation with the naturally occurring nocturnal Rubisco inhibitor 2'-carboxy-D-arabitinol 1-phosphate (CA1P), as well as with ribulose 1,5-bisphosphate (RuBP), Mg2+ and CO2. CA1P also protected Rubisco from loss of activity caused by carboxypeptidase A. When similar experiments were carried out using soluble chloroplast proteases, CA1P was again able to protect Rubisco against proteolytic degradation and the consequent irreversible loss of catalytic activity. Thus, CA1P prevents the proteolytic breakdown of Rubisco by endogenous and exogenous proteases. In this way, CA1P may affect the amounts of Rubisco protein available for photosynthetic CO2 assimilation. Rubisco turnover (in the presence of RuBP, Mg2+ and CO2) may confer similar protection against proteases in the light. (+info)
CPA3/MC-CPA Polyclonal Antibody, ALEXA FLUOR® 488 Conjugated - Bioss
Carboxypeptidase A (CPA) is a pancreatic exopeptidase which hydrolyses the peptide bond adjacent to the C-terminal end in polypeptide chains. Mast cell carboxypeptidase A (MC-CPA), a part of the peptidase M14 family, is a highly conserved metalloprotease localized to the secretory granules, along with trytases and chymases. MC-CPA is stored as an active enzyme in the granule and is released, along with other inflammatory mediators, upon mast cell degranulation. MC-CPA mirrors pancreatic carboxypeptidase A in cleaving COOH-terminal aromatic and aliphatic amino acid residues. The optimum pH of MC-CPA is between neutral and basic, depending upon the substrate. The MC-CPA gene, CPA3, resides on chromosome 3 and contains 11 exons ...
RCSB PDB - 1AYE: HUMAN PROCARBOXYPEPTIDASE A2
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Recombinant Rat Carboxypeptidase A protein (Tagged) (ab235686) | Abcam
Recombinant Rat Carboxypeptidase A protein (Tagged) is an Escherichia coli Full length protein 111 to 419 aa range, | 85% purity and validated in SDS-PAGE.
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Application of multi-block approach in the immersed boundary-lattice Boltzmann method for viscous fluid flows | [email protected]
The immersed boundary-lattice Boltzmann method was presented recently to simulate the rigid particle motion. It combines the desirable features of the lattice Boltzmann and immersed boundary methods. It uses a regular Eulerian grid for the flow domain and a Lagrangian grid for the boundary. For the lattice Boltzmann method, as compared with the single-relaxation-time collision scheme, the multi-relaxation-time collision scheme has better computational stability due to separation of the relaxations of various kinetic models, especially near the geometric singularity. So the multi-relaxation-time collision scheme is used to replace the single-relaxation-time collision scheme in the original immersed boundary-lattice Boltzmann method. In order to obtain an accurate result, very fine lattice grid is needed near the solid boundary. To reduce the computational effort, local grid refinement is adopted to offer high resolution near a solid body and to place the outer boundary far away from the body. So ...
Multi-block regression based on combinations of orthogonalisation, PLS-regression and canonical correlation analysis| Nofima
Sequence-Controlled Multi-Block Glycopolymers to Inhibit DC-SIGN-gp120 Binding - Zhang - 2013 - Angewandte Chemie International...
We acknowledge financial support from the University of Warwick and the China Scholarship Council. Equipment used in this research was funded by the Innovative Uses for Advanced Materials in the Modern World (AM2) with support from AWM and ERDF. D.M.H. is a Royal Society/Wolfson Fellow and C.R.B. is a Science City Senior Research Fellow. Dr. Christopher N. Scanlan has provided the gp120.. ...
OriGene - CPXM1 (NM 019609) cDNA Clone
CPXM1 - CPXM1 (untagged)-Human carboxypeptidase X (M14 family), member 1 (CPXM1), transcript variant 1 available for purchase from OriGene - Your Gene Company.
OriGene - CPXM1 (NM 019609) cDNA Clone
CPXM1 - CPXM1 (untagged)-Human carboxypeptidase X (M14 family), member 1 (CPXM1), transcript variant 1 available for purchase from OriGene - Your Gene Company.
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Rapid Product Development of Polyolefins - ProSensus - Multivariate Analysis Consulting for Manufacturing
The coefficients plot above indicates which X-variables have the most overall impact on the Y-variables (product quality). Each bar represents one particular X-variable. The X-variables are colour-coded according to 4 defined blocks of data. Here, it is readily observed that the orange block (Raw Materials & Blending Ratios) and green block (Properties of Raw Materials) have the most significant impact on product quality in the MVA multi-block model. Further, the purple block (Analytical Tests) provide little value, suggesting that consideration could be made to eliminate these tests and their associated costs. ...
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Vol. 24 Issue 6 | Nov-Dec 2014 | pp. 819 - 977 | EJO
Enrique Santos-Bueso, Federico Sáenz-Francés, Mercedes Serrador-García, Jesús Porta-Etessam, José María Martínez-de-la-Casa, Julián García-Feijoo, Julián García-Sánchez Eur J Ophthalmol 2014; 24(6): 960 - 963 ...
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chymotrypsin C(EC 188.8.131.52) - Creative Enzymes
Formed from pig chymotrypsinogen C, and from cattle subunit II of procarboxypeptidase A. Reacts more readily with Tos-Leu-CH2Cl than Tos-Phe-CH2Cl in contrast to chymotry
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Re: index usage
A much *simplified* example on how I teach this stuff... Lets say we have a table that has 10,000,000 rows which are stored in 1,000,000 data blocks meaning we have approximately 10 rows per block on average. Lets say we have an index on this table that has 100,000 leaf blocks meaning we have on average approximately 100 leaf entries per leaf block the index has 3 levels. Lets also say we have an effective multi-block read capability of 10 blocks per I/O (meaning Oracle will read 10 consecutive blocks at a time on average during a full table scan multiblock read). Finally, lets say were interested in accessing *just* 10% of the data (or 1,000,000 of the total 10,000,000 rows). Will Oracle use the index or wont it ? Hopefully, Ive picked an easy set of numbers to help illustrate the answer ... Firstly, to calculate the cost of using the index access path. We need to read the root block + a branch block in order to get to the first leaf block of interest. Thats 2 logical I/Os (LIOs). ...
Sepsis Easy-Read Guide | HCPA
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Análise do polimorfismo R72P do gene TP53 em paciente com carcinoma de mama ductal invasor
Introdução: O câncer de mama é a neoplasia mais freqüente e também a principal causa de morte por câncer entre as mulheres. O gene TP53 é polimórfico no códon 72 da proteína que ele codifica, podendo conter arginina (CGC) ou prolina (CCC) nesta posição. Este polimorfismo pode estar envolvido na suscetibilidade e predisposição ao câncer e apresenta uma distribuição étnica e geográfica bastante variável. O genótipo homozigoto para arginina parece ser um fator de risco e prognóstico significativo para o câncer de mama. Métodos: Extraído DNA a partir do sangue periférico de 76 pacientes consecutivas com carcinoma ductal invasor (CDI), tratadas no Serviço de Mastologia do HCPA, em qualquer estágio da doença. 80 amostras de DNA do grupo controle de doadores saudáveis do Banco de Sangue do HCPA foram incluídas de forma aleatória. Foram coletados dados demográficos e dados das características clínicas e histopatológicas e realizada a amplificação do éxon 4 do gene ...
Achados audiológicos em crianças com fissura labiopalatina de 4 a 10 anos de idade
Introdução: As fissuras labiopalatinas são resultados de malformação decorrentes de falhas no desenvolvimento ou na maturação dos processos embrionários. Objetivo: descrever os achados audiológicos em crianças com FLP, atendidas no centro de otite média do Brasil do HCPA. Métodos: A população foi composta de crianças portadoras de FLP atendidas no centro de otite média do Brasil do HCPA no período de 2007 a 2009, 55 do gênero feminino e 51 masculino, com idades entre quatro a 10 anos. Todas realizaram avaliação otorrinolaringológica e audiometria tonal. Resultados: A amostra foi composta de 106 com média de 6,2 anos (± 1,3), predominância foi sexo feminino (n=55;51%). Quando comparados os limiares das orelhas direita e esquerda houve uma diferença significativa na frequência 250Hz, na pesquisa da via aérea (p,0,001). Os valores foram mais elevados na orelha direita. Encontramos em nosso estudo um total (63%) limiares auditivos normais, (42%) perda auditiva condutiva ...
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4R)-Benzyl-4-deoxy-4-C-nitrophenyl-b-D-arabinopyranoside - BOC Sciences
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Weinert, Letícia Schwerz; Triches, Cristina Bergmann; Leitão, Cristiane Bauermann; Miltersteiner, Diego; Costa, Cezar Amauri Ribeiro da; Balbinotto, Antônio; Silveiro, Sandra Pinho; Gross, Jorge Luiz (HCPA/FAMED/UFRGS, 2007) ...
2s-2-benzyl-3-tert-butoxycarbonyl-amino-propanoic-acid | VWR
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1-benzyl-4-4-iodobenzyl-piperazine | VWR
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Overall CPA Exam Strategies | Accounting, Financial, Tax
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Difference Between CPA and Accountant | Difference Between
CPA vs Accountant CPA or Certified Public Accountant and Accountant perform almost the same duties. But the fact is that all accountants cannot be Certified
CPA Daily - Van Cao пластыри от варикоза и васкулита
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Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem...
We have cloned the cDNA for human carboxypeptidase D (CPD), a new B-type metallocarboxypeptidase that is membrane bound and has an acidic pH optimum. The 5.8 kb of cDNA sequenced contains an open reading frame of 4131 bp encoding 1377 amino acid residues. The sequence is similar (75% identity) to duck gp180, a protein that was isolated, cloned and sequenced as a hepatitis B virus-binding protein but not characterized as a carboxypeptidase. Hydropathic analysis revealed a hydrophobic region at the N-terminus, representing the signal peptide, and one near the C-terminus that probably represents the transmembrane anchor. The most striking feature is the presence of three tandem carboxypeptidase homology domains that have sequence similarity to the regulatory B-type carboxypeptidase family, typified by carboxypeptidases M, E and N. Because of the three repeats, CPD is about three times larger (175-180 kDa) than other members of this family (approx. 50-62 kDa). Domain 2 is most closely related to ...
The activation pathway of procarboxypeptidase B from porcine pancreas: Participation of the active enzyme in the proteolytic...
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 ...
Carboxypeptidases a | definition of Carboxypeptidases a by Medical dictionary
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Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: Localization to the trans-Golgi network and recycling...
TY - JOUR. T1 - Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells. T2 - Localization to the trans-Golgi network and recycling from the cell surface. AU - Varlamov, Oleg. AU - Fricker, Lloyd D.. PY - 1998. Y1 - 1998. N2 - Carboxypeptidase D (CPD) is a recently discovered membrane-bound metallocarboxypeptidase that has been proposed to be involved in the post-translational processing of peptides and proteins that transit the secretory pathway. In the present study, the intracellular distribution of CPD was examined in AtT-20 cells, a mouse anterior pituitary-derived corticotroph. Antisera to CPD stain the same intracellular structures as those labeled with furin and wheat germ agglutinin. This distribution is distinct from carboxypeptidase E, which is localized to the secretory vesicles in the cell processes. The perinuclear distribution of CPD is detected even when the AtT-20 cells are treated with brefeldin A for 1-30 minutes, suggesting that CPD is present in the ...
Association of rare chymotrypsinogen C (CTRC) gene variations in patients with idiopathic chronic pancreatitis
Extensive genetic studies of chronic pancreatitis over the past decade have highlighted the importance of a tightly regulated balance between activation and inactivation of trypsin within the pancreas to disease susceptibility and resistance. The recent identification of chymotrypsin C (CTRC) as enz …
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 ...
Assay of procarboxypeptidase U, a novel determinant of the fibrinolytic cascade, in human plasma. - Free Online Library
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
Carboxypeptidase B, For Mass Spectrometry, Recombinant Enzyme, Specific Activity 170u/mg Pro.
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Lysine Carboxypeptidase Inhibitors - Lysine Carboxypeptidase - Inhibitors and Substrates
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 substrate / V. Akparov, V. Timofeev, I. Khaliullin et al. // Journal of Biomolecular Structure and Dynamics, издательство Taylor & Francis. - 2017. Carboxypeptidase B (EC 184.108.40.206) (CPB) is commonly used in the industrial insulin production and as a template for drug design. However, its ability to discriminate substrates with hydrophobic, hydrophilic, and charged side chains is not well understood. We report structure of CPB complex with a transition state analog N-sulfamoyl-L-phenylalanine solved at 1.74Å. The study provided an insight into structural basis of CPB substrate specificity. Ligand binding is affected by structure-depended conformational changes of Asp255 in S1-subsite, interactions with Asn144 and Arg145 in C-terminal binding subsite, and Glu270 in the catalytic center. Side chain of the non-specific substrate analog SPhe in comparison with that of ...
CPE carboxypeptidase E [Homo sapiens (human)] - Gene - NCBI
This gene encodes a member of the M14 family of metallocarboxypeptidases. The encoded preproprotein is proteolytically processed to generate the mature peptidase. This peripheral membrane protein cleaves C-terminal amino acid residues and is involved in the biosynthesis of peptide hormones and neurotransmitters, including insulin. This protein may also function independently of its peptidase activity, as a neurotrophic factor that promotes neuronal survival, and as a sorting receptor that binds to regulated secretory pathway proteins, including prohormones. Mutations in this gene are implicated in type 2 diabetes. [provided by RefSeq, Nov 2015 ...
CPXM1 - Wikipedia
Probable carboxypeptidase X1 is an enzyme that in humans is encoded by the CPXM1 gene. The protein encoded by this gene is a member of the M14 family of zinc carboxypeptidases; however, the protein has no detectable carboxypeptidase activity. The encoded protein is thought to be an extracellular and/or membrane protein, and may be involved in cell-cell interactions. GRCh38: Ensembl release 89: ENSG00000088882 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000027408 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta ...
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Oligomer-beta blocker conjugates | Glycerophospholipids for the improvement of cognitive functions | Albumin conjugated temperature and pH-sensitive multi-block copolymer, a method of preparation thereof and drug... | Topical gel compositions including polycaprolactone polymer and methods for enhancing the topical application... | Method for producing a composite organic compound powder for medical use |
CPA1 - Carboxypeptidase A1 precursor - Homo sapiens (Human) - CPA1 gene & protein
Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.
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Karboksipeptidaza A - Википедија, слободна енциклопедија
Reeck, G.R., Walsh, K.A. and Neurath, H. (1971). „Isolation and characterization of carboxypeptidases A and B from activated pancreatic juice. Biochemistry. 10: 4690-4698. PMID 5140186 ...
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Enzymes: strong secretion of amylases (α-amylase and glucoamylase); some carboxypeptidase; low tyrosinase ...
Carboxypeptidases cleave at the carboxyl end of the protein. While they can catabolize proteins, they are more often used in ... "Carboxypeptidase". www.chemistry.wustl.edu. Retrieved 2019-03-23. Nelson DL, Cox MM, Lehninger AL (2013). Lehninger principles ... These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. ...
Carboxypeptidase, which is a protease that takes off the terminal amino acid group from a protein ...
CPN2: Carboxypeptidase N subunit 2. *CPOX: coproporphyrinogen oxidase (coproporphyria, harderoporphyria). *DPPA2: Developmental ...
Wang T, Parris J, Li L, Morgan JI (2006). "The carboxypeptidase-like substrate-binding site in Nna1 is essential for the rescue ... ATP/GTP binding protein 1 is gene that encodes the protein known as cytosolic carboxypeptidase 1 (CCP1), originally named NNA1 ... CCP1/NNA1 is a zinc carboxypeptidase that contains nuclear localization signals that was initially cloned from regenerating ... with alleles containing a zinc carboxypeptidase domain and an ATP/GTP binding motif, a protein first identified in alpha- ...
List of OMIM disorder codes
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 ... "Entrez Gene: CPA3 carboxypeptidase A3 (mast cell)". Reynolds DS, Gurley DS, Austen KF (January 1992). "Cloning and ...
SCPEP1: encoding enzyme Retinoid-inducible serine carboxypeptidase. *SEBOX: encoding protein SEBOX homeobox ...
Psi-loop motif from Carboxypeptidase A. Psi-loop motif. The psi-loop (Ψ-loop) motif consists of two antiparallel strands ...
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 ...
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 ... Huang H, Reed CP, Zhang JS, Shridhar V, Wang L, Smith DI (Jul 1999). "Carboxypeptidase A3 (CPA3): a novel gene highly induced ... 2005). "Detailed molecular comparison between the inhibition mode of A/B-type carboxypeptidases in the zymogen state and by the ...
... (EC 220.127.116.11, dipeptidyl carboxypeptidase (Dcp), dipeptidyl carboxypeptidase) is an enzyme. It ... Yaron A (1976). "Dipeptidyl carboxypeptidase from Escherichia coli". Methods in Enzymology. 45: 599-610. doi:10.1016/s0076-6879 ... Conlin CA, Miller CG (1995). "Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium ...
Carboxypeptidase, a hydrolytic enzyme important in digestion. Another complex ion enzyme is catalase, which decomposes the ...
Thomas A. Steitz
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 ... Chen J, Streb JW, Maltby KM, Kitchen CM, Miano JM (Sep 2001). "Cloning of a novel retinoid-inducible serine carboxypeptidase ... "Entrez Gene: SCPEP1 serine carboxypeptidase 1". Robb GB, Rana TM (2007). "RNA helicase A interacts with RISC in human cells and ...
Carboxypeptidase A (left) was the first protein structure from Lipscomb's group. Carboxypeptidase A is a digestive enzyme, a ... Carboxypeptidase A digests by chopping off certain amino acids one-by-one from one end of a protein. The size of this structure ... "The Structure of Carboxypeptidase A, IV. Prelimitary Results at 2.8 A Resolution, and a Substrate Complex at 6 A Resolution". ... Carboxypeptidase A was a much larger molecule than anything solved previously. Aspartate carbamoyltransferase. (right) was the ...
List of biophysically important macromolecular crystal structures
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, ...
"Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation". Science. 358 (6369): 1448-1453. ...
Protein BM-1 bahasa Indonesia, ensiklopedia bebas
... procollagen carboxypeptidase; procollagen carboxy-terminal proteinase; procollagen peptidase, BMP-1, EC 18.104.22.168) merupakan ...
... produces streptomycin II and carboxypeptidase. List of Streptomyces species LPSN bacterio.net ... "Carboxypeptidase from Streptomyces bikiniensis: Primary structure, isolation, and properties". Biochemistry (Moscow). 75 (8): ...
"Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, ... 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 ... Nagae A, Deddish PA, Becker RP, Anderson CH, Abe M, Tan F, Skidgel RA, Erdös EG (December 1992). "Carboxypeptidase M in brain ...
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: ...
However, carboxypeptidases do not have something similar to the C-domain. In carboxypeptidase A, the active site is accessible ...
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 ...
Carboxypeptidase T - Wikipedia
Carboxypeptidase T (EC 22.214.171.124, CPT) is an enzyme. 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- ...
Carboxypeptidase - Wikipedia
... 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 ...
Zinc 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 126.96.36.199, 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". ...
Muramoyltetrapeptide carboxypeptidase - Wikipedia
... 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) Biology portal. ... Metz R, Henning S, Hammes WP (March 1986). "LD-carboxypeptidase activity in Escherichia coli. II. Isolation, purification and ... DasGupta H, Fan DP (July 1979). "Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium ...
This article focuses on four human carboxypeptidases (CPs): two metallo-CPs and two serine CPs. The metallo-CPs are members of ... Cellular carboxypeptidases Immunol Rev. 1998 Feb;161:129-41. doi: 10.1111/j.1600-065x.1998.tb01577.x. ... This article focuses on four human carboxypeptidases (CPs): two metallo-CPs and two serine CPs. The metallo-CPs are members of ...
Carboxypeptidase B2 (IPR033849) | InterPro | EMBL-EBI
Carboxypeptidase A definition | Drugs.com
Patent US6780640 - Human carboxypeptidases and polynucleotides encoding the same - Google Patents
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 ...
Escherichia coli mutants defective in dipeptidyl carboxypeptidase | PNAS
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 188.8.131.52 ...
Carboxypeptidase - definition of carboxypeptidase by The Free Dictionary
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 ...
Carboxypeptidase E, carboxypeptidase domain (IPR034232) | InterPro | EMBL-EBI
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 ...
Dipeptidyl carboxypeptidase | Definition of Dipeptidyl carboxypeptidase at Dictionary.com
Rapid Epitope Mapping by Carboxypeptidase Digestion and Immunoblotting | SpringerLink
Carboxypeptidase P - Selective Proteolytic Enzymes | Sigma-Aldrich