Relevant bibliographies by topics / Carboxypeptidase A

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Carboxypeptidase A'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "Carboxypeptidase A"

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Fan, Xuemo, Sandy J. Olson, Lewis S. Blevins, George S. Allen, and Mahlon D. Johnson. "Immunohistochemical Localization of Carboxypeptidases D, E, and Z in Pituitary Adenomas and Normal Human Pituitary." Journal of Histochemistry & Cytochemistry 50, no. 11 (November 2002): 1509–15. http://dx.doi.org/10.1177/002215540205001111.

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Carboxypeptidases may play important role(s) in prohormone processing in normal and neoplastic adenohypophyseal cells of the pituitary. We have recently demonstrated carboxypeptidase E (CPE) and carboxypeptidase Z (CPZ) in the majority of adenohypophyseal cells with carboxypeptidase D (CPD) immunoreactivity largely confined to adrenocorticotrophs. This study evaluated the expression patterns of CPE, CPD, and CPZ immunoreactivity in 48 pituitary adenomas. Our immunohistochemistry demonstrated extensive intracytoplasmic immunoreactivity for CPE, CPD, and CPZ in adrenocorticotrophic hormone (ACTH)-producing adrenocorticotroph cells, prolactin-producing lactotroph cells, and growth hormone (GH)-producing somatotroph cell adenomas, all of which require carboxypeptide processing of prohormones to produce active endocrine hormones. In contrast to the restricted expression in the normal adenohypophysis, CPD appeared to be widespread in the majority of adenomas, suggesting that CPD levels are increased in adenomas. In luteinizing hormone/follicle-stimulating hormone (LH/FSH)-producing gonadotroph adenomas, which do not require carboxypeptidases to produce gonadotropins, only CPZ immunostaining was demonstrated. In null-cell adenomas, CPE immunoreactivity was detected in the majority of tumors, but CPD and CPZ were identified only in a minority of cases. CPE in these cells may process other peptides critical for pituitary cell function, such as chromogranin A or B. These findings suggest that CPs participate in the functioning of pituitary adenomas.
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Greene, D., B. Das, and L. D. Fricker. "Regulation of carboxypeptidase E. Effect of pH, temperature and Co2+ on kinetic parameters of substrate hydrolysis." Biochemical Journal 285, no. 2 (July 15, 1992): 613–18. http://dx.doi.org/10.1042/bj2850613.

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Carboxypeptidase E is a member of the carboxypeptidase A and B gene family, with many of the putative active-site and substrate-binding residues conserved between these enzymes. However, the pH optimum of carboxypeptidase E is substantially lower than that of carboxypeptidases A and B. To evaluate whether the difference in the pH optima of these carboxypeptidases reflects fundamental differences in the ionization behaviour of active-site residues, the influence of pH on carboxypeptidase E activity was examined. The V(max) for hydrolysis of dansyl-Phe-Ala-Arg is pH-independent between 5 and 7, but decreases at pH values below 5. The pKa for the group the protonation of which leads to the loss of activity is approximately 4.8, and the slope of the V(max.)/pH profile suggests that only a single ionizable group is involved. In contrast, Km and V(max.)/Km are dramatically influenced by pH over the range 5-7, with multiple ionizable groups detected in this pH range. The pKa of the group the protonation of which decreases the V(max.) of substrate hydrolysis is lower (4.5) for carboxypeptidase E which had been reconstituted with Co2+. The enthalpy of ionization of the group observed in the V(max.) profile for carboxypeptidase E is approx. 28.9 kJ/mol. These results are compatible with the active-site model of the homologous carboxypeptidase A: in this model the ionization of a metal-bound water molecule is responsible for the observed decrease in V(max.).
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Deddish, P. A., R. A. Skidgel, and E. G. Erdös. "Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase)." Biochemical Journal 261, no. 1 (July 1, 1989): 289–91. http://dx.doi.org/10.1042/bj2610289.

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Carboxypeptidases H and M differ in their distribution and other properties, but both are activated by Co2+ and inhibited by guanidinoethylmercaptosuccinic acid. The higher degree of activation or inhibition of carboxypeptidase H by these agents at acid pH has been employed to identify this enzyme in tissues. We found that the activation or inhibition of both purified and plasma-membrane-bound human carboxy-peptidase M depends on the pH of the medium. CoCl2 activated over 6-fold at pH 5.5, but less than 2-fold at pH 7.5. Guanidinoethylmercaptosuccinic acid inhibited the membrane-bound carboxypeptidase M more effectively than the purified enzyme, and the IC50 was about 25-30 times lower at pH 5.5. As purified human plasma carboxypeptidase N and pancreatic carboxypeptidase B were also activated more at pH 5.5, we conclude that the increased activation by CoCl2 is due to the enhanced dissociation of Zn2+ below the pKa of the ligands that co-ordinate the cofactor in the protein. Thus increased activation or inhibition at acid pH would not differentiate basic carboxypeptidases.
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Vitols, Karin S., Yolanda D. Montejano, Ulrike Kuefner, and F. M. Huennekens. "Selective Cytotoxicity of Carboxypeptidase-activated Methotrexate ex-Peptides." Pteridines 1, no. 1 (February 1989): 65–69. http://dx.doi.org/10.1515/pteridines.1989.1.1.65.

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Summary Methotrexate ex-pep tides (derivatives in which an amino acid is linked covalently to the ex-carboxyl of the glutamate residue on the parent drug) can be hydrolyzed by specific carboxypeptidases to yield free Methotrexate (MTX) and the corresponding amino acid. Studies with L12l0 cells in suspension culture have shown that the MTX pep tides can serve as "pro-drugs": Because of their inability to be taken up by cells, they are relatively non-toxic. When co-administered with appropriate carboxypeptidases, however, they become equitoxic with MTX. In the present investigation, the potential of the MTX-ala/carboxypeptidase A combination for providing regional cytotoxicity was demonstrated in a model system involving L12l0 cells propagated in semi-solid agarose. When cells and one of the components (MTX peptide or carboxypeptidase) were distributed uniformly throughout the agarose, and the other component was immobilized at the center, a discrete zone of cell kill radiated from the fixed component. These results suggest the possibility of developing a new mode of cancer chemotherapy involving circulating MTX peptides in conjunction with carboxypeptidases linked covalently to tumor-targeted monoclonal antibodies.
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Kimura, Yoshio, Yukie Takashima, Yushi Tokumasu, and Masayuki Sato. "Molecular Cloning, Sequence Analysis, and Characterization of a Penicillin-Resistantdd-Carboxypeptidase of Myxococcus xanthus." Journal of Bacteriology 181, no. 15 (August 1, 1999): 4696–99. http://dx.doi.org/10.1128/jb.181.15.4696-4699.1999.

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ABSTRACT We have cloned a gene, pdcA, from the genomic library of Myxococcus xanthus with an oligonucleotide probe representing conserved regions of penicillin-resistantdd-carboxypeptidases. The amino- and carboxy-terminal halves of the predicted pdcA gene product showed significant sequence similarity toN-acetylmuramoyl-l-alanine amidase and penicillin-resistant dd-carboxypeptidase, respectively. ThepdcA gene was expressed in Escherichia coli, and the characteristics of the gene product were similar to those ofdd-carboxypeptidase (VanY) of vancomycin-resistant enterococci. No apparent changes in cell growth, sporulation, or germination were observed in pdcA deletion mutants.
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Ishikawa, Kazuhiko, Hiroyasu Ishida, Ikuo Matsui, Yutaka Kawarabayasi, and Hisasi Kikuchi. "Novel Bifunctional Hyperthermostable Carboxypeptidase/Aminoacylase from Pyrococcus horikoshii OT3." Applied and Environmental Microbiology 67, no. 2 (February 1, 2001): 673–79. http://dx.doi.org/10.1128/aem.67.2.673-679.2001.

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ABSTRACT Genome sequencing of the thermophilic archaeon Pyrococcus horikoshii OT3 revealed a gene which had high sequence similarity to the gene encoding the carboxypeptidase ofSulfolobus solfataricus and also to that encoding the aminoacylase from Bacillus stearothermophilus. The gene from P. horikoshii comprises an open reading frame of 1,164 bp with an ATG initiation codon and a TGA termination codon, encoding a 43,058-Da protein of 387 amino acid residues. However, some of the proposed active-site residues for carboxypeptidase were not found in this gene. The gene was overexpressed in Escherichia coli with the pET vector system, and the expressed enzyme had high hydrolytic activity for both carboxypeptidase and aminoacylase at high temperatures. The enzyme was stable at 90°C, with the highest activity above 95°C. The enzyme contained one bound zinc ion per one molecule that was essential for the activity. The results of site-directed mutagenesis of Glu367, which corresponds to the essential Glu270 in bovine carboxypeptidase A and the essential Glu in other known carboxypeptidases, revealed that Glu367 was not essential for this enzyme. The results of chemical modification of the SH group and site-directed mutagenesis of Cys102 indicated that Cys102 was located at the active site and was related to the activity. From these findings, it was proven that this enzyme is a hyperthermostable, bifunctional, new zinc-dependent metalloenzyme which is structurally similar to carboxypeptidase but whose hydrolytic mechanism is similar to that of aminoacylase. Some characteristics of this enzyme suggested that carboxypeptidase and aminoacylase might have evolved from a common origin.
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TAN, Fulong, Michael REHLI, Stefan W. KRAUSE, and Randal A. SKIDGEL. "Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains." Biochemical Journal 327, no. 1 (October 1, 1997): 81–87. http://dx.doi.org/10.1042/bj3270081.

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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 carboxypeptidases M, E and N (45–48% identity), followed by domain 1 (37–38%) and domain 3 (20–27%). There is much higher sequence identity in regions containing putative active site residues, and all catalytically important residues are strictly conserved in domains 1 and 2. In domain 3, however, only 1 of 8 active site residues is conserved, indicating that this portion might not be catalytically active. Northern blotting of mRNA from human tissues and cells showed high levels of CPD mRNA in placenta, pancreas and Hep G2 hepatoma cells, and smaller amounts in skeletal muscle, heart and HT-29 colon carcinoma and melanoma cell lines.
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Vilanova, M., J. Vendrell, M. T. López, C. M. Cuchillo, and F. X. Avilés. "Preparative isolation of the two forms of pig pancreatic pro-(carboxypeptidase A) and their monomeric carboxypeptidases A." Biochemical Journal 229, no. 3 (August 1, 1985): 605–9. http://dx.doi.org/10.1042/bj2290605.

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A method is reported for the preparative isolation of the two forms of pro-(carboxypeptidase A) from pig pancreas: the monomer and the binary complex with pro-(proteinase E). This method, which is mainly based on chromatography on DEAE-Sepharose at pH 5.7, allows these proenzymes to be prepared more quickly and in safer conditions than with other reported methods. Undegraded and homogeneous carboxypeptidase A1 and A2 species (peptidyl-L-amino acid hydrolase, EC 3.4.17.1), in monomeric forms with high specific activity, are also obtained in high yield by controlled trypsin activation of either of the pro-(carboxypeptidases A) followed by chromatography on DEAE-Sepharose at pH 5.8 under dissociating conditions (7 M-urea).
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Masuda, Kaname, Masami Yoshioka, Daisuke Hinode, and Ryo Nakamura. "Purification and Characterization of Arginine Carboxypeptidase Produced by Porphyromonas gingivalis." Infection and Immunity 70, no. 4 (April 2002): 1807–15. http://dx.doi.org/10.1128/iai.70.4.1807-1815.2002.

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ABSTRACT Arginine carboxypeptidase was isolated from the cytoplasm of Porphyromonas gingivalis 381 and purified by DEAE-Sephacel column chromatography, followed by high-performance liquid chromatography on DEAE-5PW and TSK G2000SWXL. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme revealed the presence of three major bands at 42, 33, and 32 kDa with identical N-terminal sequences. By Western blotting analysis and immunoelectron microscopy, the arginine carboxypeptidase was found to be widely distributed in the cytoplasm and on the surface of the outer membrane. The open reading frame corresponding to the N-terminal amino acids of the arginine carboxypeptidase was detected by a search of the sequence of the P. gingivalis W83 genome. This sequence showed homology with mammalian carboxypeptidases (M, N, and E/H) and included a zinc-binding region signature, suggesting that the enzyme is a member of the zinc carboxypeptidase family. The purified enzyme was inhibited by EGTA, o-phenanthroline, dl-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, and some metal ions, such as Cu2+, Zn2+, and Cd2+. On the other hand, Co2+ activated the enzyme. The enzyme released arginine and/or lysine from biologically active peptides containing these amino acids at the C terminus but did not cleave substrates when proline was present at the penultimate position. These results indicate that the arginine carboxypeptidase produced by P. gingivalis is an exo type of metallocarboxypeptidase. This enzyme may function to release arginine in collaboration with an arginine aminopeptidase, e.g., Arg-gingipain, to obtain specific amino acids from host tissues during the growth of P. gingivalis.
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Shevchenko, K. V., L. A. Andreeva, I. Yu Nagaev, V. P. Shevchenko, and N. F. Myasoedov. "Study of stability of proline-containing derivatives of dopamine and serotonin in the biological media in vitro experiments." Biomeditsinskaya Khimiya 65, no. 6 (2019): 498–506. http://dx.doi.org/10.18097/pbmc20196506498.

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Boc-Gly-Pro-DP, Z-Gly-Pro-DP, LA-Gly-Pro-DP, Boc-Gly-Pro-Srt, Z-Gly-Pro-Srt were synthesized for the first time. The stability of these compounds in the presence of leucine aminopeptidase, carboxypeptidase Y, carboxypeptidase B and proline endopeptidase (PEP) was determined. It turned out that the compounds are stable in the presence of aminopeptidases and carboxypeptidases. In the presence of PEP, dopamine (DP) and serotonin (Srt) are cleaved from the synthesized preparations. Thus, new proline-containing Srt and DP derivatives were obtained, Srt and DP could be gradually released from them. This suggest the possibility of a prolonged action of these biologically active compounds on the vital activity of cells and, consequently, of the whole organism.
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Dissertations / Theses on the topic "Carboxypeptidase A"

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Commeinhes, Frédéric. "Structure tridimentionnelle de la carboxypeptidase A par diffraction des rayons X." Paris 5, 1994. http://www.theses.fr/1994PA05P019.

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Rowsell, Sian. "Crystal structure of carboxypeptidase G←2." Thesis, Imperial College London, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.362421.

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Küchenthal, Christian-Hubertus [Verfasser]. "Synthese neuartiger krebsspezifischer Carboxypeptidase-Liganden / Christian-Hubertus Küchenthal." Gießen : Universitätsbibliothek, 2012. http://d-nb.info/1063954940/34.

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Lehouritis, Panos. "Bacterial directed enzyme prodrug therapy using carboxypeptidase G2." Thesis, Institute of Cancer Research (University Of London), 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.429988.

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Bleakman, Alexandra. "Processing of the oxytocin precursor by carboxypeptidase E." Thesis, University of Bath, 1990. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.279168.

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Nakase, Hiroshi. "Action Mode and Subsite Properties of Carboxypeptidase Y." Kyoto University, 2000. http://hdl.handle.net/2433/151622.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第8627号
農博第1154号
新制||農||814(附属図書館)
学位論文||H12||N3472(農学部図書室)
UT51-2000-R33
京都大学大学院農学研究科応用生命科学専攻
(主査)教授 林 力丸, 教授 池田 篤治, 教授 加藤 暢夫
学位規則第4条第1項該当
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Arndt, Joseph W. "Characterization and structural determination of metalloenzymes DNA polymerase beta, carboxypeptidase, and acetyl coenzyme-A decarbonylase/synthase /." Columbus, OH : Ohio State University, 2003. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1061312369.

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Thesis (Ph. D.)--Ohio State University, 2003.
Title from first page of PDF file. Document formatted into pages; contains xxii, 172 p. : ill., some col. Includes abstract and vita. Advisor: Michael K. Chan, Dept. of Chemistry. Includes bibliographical references (p. 165-172).
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Transfiguracion, Julia de la Cruz. "Purification and characterization of carboxypeptidase Y from Kluyveromyces fragilis." Thesis, McGill University, 1994. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=22527.

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Carboxypeptidase Y (E.C. 3.4.12.1) was produced from Kluyveromyces fragilis ATCC 28244. The maximum growth and enzyme production were obtained during 24 hr of growth at the late logarithmic phase with optimized conditions (25$ sp circ $C, 300 rpm, pH 5) using YPD (1% yeast extract, 2% peptone, 2% dextrose, w/v) broth medium. A Fast Protein Liquid Chromatography (FPLC) was used for the enzyme purification. The enzyme was purified to 216 fold over the crude extract with a recovery of 18%. The apparent molecular weight of the purified enzyme was estimated to be 120 kDa on Native-PAGE and 56 kDa on SDS-PAGE suggesting that carboxypeptidase Y from Kluyveromyces fragilis consists of two subunits. The pH and temperature optima of the enzyme were pH 6.0 and 35$ sp circ$C, respectively. The enzyme activity was strongly inhibited by diisopropylphosphofluoridate (DIPF) and phenylmethylsulfonylfluoride (PMSF), and caused an average 50% loss of activity when incubated with various metal cations.
The apparent K$ sb{ rm m}$ and V$ sb{ rm max}$ values obtained for n-benzoyl-L-tyrosine-p-nitroanilide (BTPNA) and carboxybenzoxyphenylalanylalanine (Cbz-Phe-Ala) were 5.1 mM and 13.4 $ mu$mole/min/mg and 2.98 mM and 22.58 $ mu$mole/min/mg, respectively. Carboxypeptidase Y hydrolysis on the tryptic digests of $ alpha sb{ rm s1}$- and $ beta$-casein showed that the enzyme randomly removed five and three hydrophobic peptides, respectively and greatly reduced the size and heights of the other peptides analysed on Reversed Phase-High Performance Liquid Chromatography (RP-HPLC).
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Möller, Carsten. "Carboxypeptidase Z und Lix1 in der Embryogenese der Vertebraten." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=969730136.

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Fonrose, Xavier. "Recherche et caractérisation d'inhibiteurs de la tubuline carboxypeptidase (TCP)." Université Joseph Fourier (Grenoble), 2008. http://www.theses.fr/2008GRE10072.

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Au cours du cycle de détyrosination tyrosination, la tyrosine C-terminale de la sous-unité alpha de la tubuline est clivée par une tubuline carboxypeptidase (TCP) inconnue, puis re-ajoutée par la tubuline tyrosine ligase (TIL). L'accumulation de tubuline détyrosinée, consécutive à la perte de la TTL, est un événement fréquent et de mauvais pronostic dans plusieurs types de cancers. Cette accumulation peut être supprimée par des inhibiteurs de la TCP. Ces inhibiteurs pourraient interférer avec la progression tumorale, être utilisés pour purifier la TCP. Ces inhibiteurs ont été recherchés par criblage automatisé de molécules chimiques, à l'aide d'un test cellulaire de l'activité TCP. Nous avons pu sélectionner plusieurs molécules chimiques, de structures différentes, inhibant spécifiquement l'activité TCP. Parmi ces molécules figure le parthénolide, connu pour ces activités anti-cancéreuses. Son action inhibitrice vis-à-vis de la TCP pourrait participer à ces propriétés anti-cancéreuses
Tubulin can be cyclically modified on its alpha-subunit by enzymatic removal of the COOH-terminal tyrosine residue by tubulin carboxypeptidase (TCP) and its readdition by tubulin tyrosine ligase (TIL). Accumulation of detyrosinated tubulin is frequent in human cancers of poor prognosis. Thus, TCP could be a target for developing novel therapeutic strategies for cancers. Inhibitors of TCP, by reversing abnormal detyrosinated tubulin accumulation in tumor cells, could impair tumor progression. TCP has never been isolated and this has hampered search of specific inhibitors. We develop a cell-based assay of TCP activity and its use to screen two libraries of chemical compounds for their inhibitory potency. This led to the isolation of several compounds, not structurally related. Among them, parthenolide can efficiently inhibit TCP. Parthenolide is known for its anticancer properties. Thus, TCP inhibition could be one of the underlying mechanisms of these anticancer properties
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Books on the topic "Carboxypeptidase A"

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Tessarolo, Diane. HPLC assisted assay for carboxypeptidase U. Sudbury, Ont: Laurentian University, 1996.

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Agbaru, Adanma. Carboxypeptidase U and N in rat serum. Sudbury, Ont: Laurentian University, Department of Biology, 1993.

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Certossi, Susan Maria. Identification of creative kinase conversion factor as carboxypeptidase N. [s.l: s.n.], 1987.

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Sproule, Laurie Kathleen. Carboxypeptidase N and U in myocardial infarct and angina patients. [s.l: s.n.], 1992.

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Portelance, Eric. The effect of carboxypeptidase N on small cell lung carcinoma cells. Sudbury, Ont: Laurentian University, 1991.

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Harrison, Pierre. Studies on the stabilization and purification of human serum carboxypeptidase U. Sudbury, Ont: Laurentian University Press, 1995.

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Harrison, Pierre. High performance liquid chromatography determination of carboxypeptidase N activity in human serum. Sudbury, Ont: Laurentian University, 1990.

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Souris, John. Synthesis of a potential bi-product analogue inhibitor for human plasma carboxypeptidase N. Sudbury, Ont: Laurentian University, 1985.

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Fry, Jeffrey Lynne. Reversible modification of carboxypeptidase A by organic sulfonates, carboxylates and a tetrazolate. 1990.

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Allen, Ann Marie. A study of inhibitor binding to the active site of carboxypeptidase A. 1986.

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Book chapters on the topic "Carboxypeptidase A"

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Schomburg, Dietmar, and Dörte Stephan. "Carboxypeptidase C." In Enzyme Handbook 15, 453–62. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_100.

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Schomburg, Dietmar, and Dörte Stephan. "Carboxypeptidase D." In Enzyme Handbook 15, 463–67. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_101.

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Schomburg, Dietmar, and Dörte Stephan. "Glutamate carboxypeptidase." In Enzyme Handbook 15, 469–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_102.

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Schomburg, Dietmar, and Dörte Stephan. "Carboxypeptidase M." In Enzyme Handbook 15, 475–78. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_103.

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Schomburg, Dietmar, and Dörte Stephan. "Muramoyltetrapeptide carboxypeptidase." In Enzyme Handbook 15, 479–82. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_104.

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Schomburg, Dietmar, and Dörte Stephan. "Carboxypeptidase A2." In Enzyme Handbook 15, 487–89. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_106.

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Schomburg, Dietmar, and Dörte Stephan. "Carboxypeptidase T." In Enzyme Handbook 15, 499–502. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_109.

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Schomburg, Dietmar, and Dörte Stephan. "Carboxypeptidase Taq." In Enzyme Handbook 15, 503–6. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_110.

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Peters, Nils, Martin Dichgans, Sankar Surendran, Josep M. Argilés, Francisco J. López-Soriano, Sílvia Busquets, Klaus Dittmann, et al. "Carboxypeptidase B2, Plasma." In Encyclopedia of Molecular Mechanisms of Disease, 270–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_6977.

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Schomburg, Dietmar, and Dörte Stephan. "Tubulinyl-Tyr carboxypeptidase." In Enzyme Handbook 15, 495–97. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_108.

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Conference papers on the topic "Carboxypeptidase A"

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Johnston, Richard A., Ramon X. Barreno, Paul H. Dahm, and Ikram U. Haque. "Allergic Pulmonary Responses In Obese Carboxypeptidase E (CPE)-Deficient Mice." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2666.

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2

"Purification of a multimeric enzyme carboxypeptidase G2 by intein-mediated protein splicing." In International Conference on Medicine, Public Health and Biological Sciences. CASRP Publishing Company, Ltd. Uk, 2016. http://dx.doi.org/10.18869/mphbs.2016.143.

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ZHAO, Dan, Ya-kun ZHANG, Xiao-ping YAN, Wei GUO, and Xiao-min LIU. "Characterization of a Serine Carboxypeptidase Hoscp from Holotrichia Oblita Faldermann (Coleoptera: Scarabaeoidea)." In 2nd International Conference on Biomedical and Biological Engineering 2017 (BBE 2017). Paris, France: Atlantis Press, 2017. http://dx.doi.org/10.2991/bbe-17.2017.21.

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4

Hu, Ye. "Abstract 2507: Circulating proteolytic products of carboxypeptidase N for early detection of breast cancer." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2507.

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5

Huan, X., Y. Legrand, J. Soria, C. Soria, J. Caen, and J. Fareed. "STUDIES ON THE ANTITHROMBOTIC ACTIONS OF A COLLAGEN PEPTIDE IN A DEFINED MODEL OF VENOUS THROMBOSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644496.

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Abstract:
The synthesis and biologic actions of a collagen peptide Lys-Pro-Gly-Glu-Pro-Gly-Pro-Lys (CP) were first reported by Fauvel, et. al. in 1979. This peptide was found to inhibit collagen induced aggregation of platelets and to modulate clot formation and specific collagen induced fibrinogen binding by platelets. CP exhibited antithrombotic actions in a modified venous stasis thrombosis model (rabbit) against defined thrombogenic challenges, (ED50;(IV) 0.5 − 2.5 mg/kg; (SC) 2.5 − 7.5 mg/kg). The antithrombotic actions of this peptide exhibited a short half-life (10 minutes) after IV administration. Preincubation of this peptide with trypsin, carboxypeptidase A, carboxypeptidase B and pancreatic protease complex resulted in a loss of the antithrombotic action. Specific protease inhibitors were found to protect the peptide from this degradation effect. CP did not exert any effect on the routinely performed global coagulant and antiprotease tests at concentrations which produce antithrombotic actions (0.5 − 5 mg/kg). CP was found to synergize the antithrombotic action of heparin in both intravenous and subcutaneous routes. Preliminary studies on the mechanism of the antithrombotic actions of collagen peptide suggest these actions may be independent of effects on platelets. These studies also suggest that an oligopeptide containing arginine and lysine residues, mimicing serine protease susceptible sites, is capable of producing antithrombotic effects in an animal model of venous thrombosis.
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Schissel, SL, RW Shine, RD Brown, MA Perrella, and MD Layne. "Aortic Carboxypeptidase-Like Protein, a Discoidin Domain Protein, Regulates Lung Fibroblast Lamellipodia Formation and Collagen Contraction." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3486.

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7

Rather, Gulam M., John E. Kerrigan, Kathleen W. Scotto, and Joseph R. Bertino. "Abstract 3981: Enhancement of the anticancer activity of methylenetetrahydrofolate dehydrogenase knockdown by folate depletion with carboxypeptidase G2." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3981.

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8

Jiang, Shun-Yuan, Fu-Ming Tsai, Rong-Yaun Shyu, Chang-Chieh Wu, Tzung-Chieh Tsai, and Chun-Hua Wang. "Abstract 501: The carboxypeptidase inhibitor TIG1 interacts with cathepsin L2 and inhibits cathepsin L2-stimulated cellular invasion." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-501.

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9

Murthy, Saravana R. K., Terence K. Lee, Niamh X. Cawley, Stephen M. Hewitt, Karel Pacak, and Peng Loh. "Abstract 5327: An N-terminal truncated carboxypeptidase E splice isoform induces metastasis by activating nedd9 and other metastasis inducing genes." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-5327.

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10

Ith, B., I. Rosas, MA Perrella, MD Layne, and SL Schissel. "Aortic Carboxypeptidase-Like Protein, a Novel Collagen-Associated Protein, Is Expressed in Fibrotic Lung from Patients with Idiopathic Pulmonary Fibrosis." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3021.

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