An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from beta-lipotropin60-65.
about
60 YEARS OF POMC: Biosynthesis, trafficking, and secretion of pro-opiomelanocortin-derived peptidesRole of pGlu-serpinin, a novel chromogranin A-derived peptide in inhibition of cell deathCathepsin L participates in the production of neuropeptide Y in secretory vesicles, demonstrated by protease gene knockout and expressionPosttranslational Processing of the Neurotensin/Neuromedin-N PrecursorAminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modellingAminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase.Cathepsin L and Arg/Lys aminopeptidase: a distinct prohormone processing pathway for the biosynthesis of peptide neurotransmitters and hormones.Major role of cathepsin L for producing the peptide hormones ACTH, beta-endorphin, and alpha-MSH, illustrated by protease gene knockout and expressionProteases for processing proneuropeptides into peptide neurotransmitters and hormones.Zinc regulation of aminopeptidase B involved in neuropeptide production.Peptide precursor processing enzymes within secretory vesicles.Precursors to regulatory peptides: their proteolytic processing.The processing of peptide precursors. 'Proline-directed arginyl cleavage' and other monobasic processing mechanisms.Two novel metallopeptidases with a specificity for basic residues: functional properties, structure and cellular distribution.Processing and secretion in the neurohypophysis. Stability of isolated secretory vesicles and role of internal pH.alpha-Melanocyte-stimulating-hormone precursors in the pig pituitary.Changes in Proteases, Antiproteases and Bioactive Proteins From Mother's Breast Milk to the Premature Infant Stomach.Regulated secretion of pro-opiomelanocortin converting enzyme and an aminopeptidase B-like enzyme from dispersed bovine intermediate lobe pituitary cells.Cathepsin L expression is directed to secretory vesicles for enkephalin neuropeptide biosynthesis and secretion.Secretory vesicle aminopeptidase B related to neuropeptide processing: molecular identification and subcellular localization to enkephalin- and NPY-containing chromaffin granules.Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Enzyme Nomenclature. Recommendations 1992. Supplement 4: corrections and additions (1997).
P2860
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P2860
An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from beta-lipotropin60-65.
description
1984 nî lūn-bûn
@nan
1984 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1984 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1984年の論文
@ja
1984年論文
@yue
1984年論文
@zh-hant
1984年論文
@zh-hk
1984年論文
@zh-mo
1984年論文
@zh-tw
1984年论文
@wuu
name
An aminopeptidase activity in ...... ine from beta-lipotropin60-65.
@ast
An aminopeptidase activity in ...... ine from beta-lipotropin60-65.
@en
An aminopeptidase activity in ...... ine from beta-lipotropin60-65.
@nl
type
label
An aminopeptidase activity in ...... ine from beta-lipotropin60-65.
@ast
An aminopeptidase activity in ...... ine from beta-lipotropin60-65.
@en
An aminopeptidase activity in ...... ine from beta-lipotropin60-65.
@nl
prefLabel
An aminopeptidase activity in ...... ine from beta-lipotropin60-65.
@ast
An aminopeptidase activity in ...... ine from beta-lipotropin60-65.
@en
An aminopeptidase activity in ...... ine from beta-lipotropin60-65.
@nl
P2093
P2860
P1433
P1476
An aminopeptidase activity in ...... ine from beta-lipotropin60-65.
@en
P2093
P2860
P304
P356
10.1016/0014-5793(84)80586-4
P407
P577
1984-09-01T00:00:00Z