Carboxypeptidase H
"Carboxypeptidase H" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
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.
Descriptor ID |
D043423
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MeSH Number(s) |
D08.811.277.656.350.245.167 D08.811.277.656.350.555.250 D08.811.277.656.675.555.250 D08.811.277.656.837.124
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Concept/Terms |
Carboxypeptidase H- Carboxypeptidase H
- Enkephalin-Synthesizing Carboxypeptidase
- Carboxypeptidase, Enkephalin-Synthesizing
- Enkephalin Synthesizing Carboxypeptidase
- Enkephalin-Forming Carboxypeptidase
- Carboxypeptidase, Enkephalin-Forming
- Enkephalin Forming Carboxypeptidase
- Carboxypeptidase E
- Enkephalin Convertase
- Convertase, Enkephalin
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Below are MeSH descriptors whose meaning is more general than "Carboxypeptidase H".
Below are MeSH descriptors whose meaning is more specific than "Carboxypeptidase H".
This graph shows the total number of publications written about "Carboxypeptidase H" by people in this website by year, and whether "Carboxypeptidase H" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2004 | 0 | 1 | 1 |
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Below are the most recent publications written about "Carboxypeptidase H" by people in Profiles.
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Zhang DM, Zhou ZG, Weng JP, Li LR, Deng H, Zhang C, Jin P, Huang G, Peng J, Xiu LL, Wang JP, Yang L. [Etiological dissection in common anti-islet autoantibody-negative patients with type 1 diabetes]. Zhonghua Yi Xue Za Zhi. 2004 Aug 02; 84(15):1247-51.
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Davidson HW. (Pro)Insulin processing: a historical perspective. Cell Biochem Biophys. 2004; 40(3 Suppl):143-58.
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Guest PC, Ravazzola M, Davidson HW, Orci L, Hutton JC. Molecular heterogeneity and cellular localization of carboxypeptidase H in the islets of Langerhans. Endocrinology. 1991 Aug; 129(2):734-40.
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Davidson HW, Hutton JC. The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing. Biochem J. 1987 Jul 15; 245(2):575-82.
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Hutton JC, Davidson HW, Peshavaria M. Proteolytic processing of chromogranin A in purified insulin granules. Formation of a 20 kDa N-terminal fragment (betagranin) by the concerted action of a Ca2+-dependent endopeptidase and carboxypeptidase H (EC 3.4.17.10). Biochem J. 1987 Jun 01; 244(2):457-64.
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