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- W2000657836 abstract "Peptide hormones are synthesized from larger precursors by cleavages at paired basic residues. We have isolated a pro-hormone converting enzyme from bovine neural and intermediate lobe secretory vesicles that cleaves pro-vasopressin and pro-opiomelanocortin at Lys-Arg residues to yield vasopressin, and adrenocorticotropin/endorphin-related peptides, respectively. The enzyme from both lobes is an aspartyl protease of ~́ 70 000 Da, is a glycoprotein and has an optimum pH range of 4.0–5.0. Present within the same secretory vesicles is an aminopeptidase B-like enzyme which is a metalloprotease that is inhibited by Co2+ and Zn2+. This enzyme may play a role in trimming off the N-terminal extended basic residues from peptides liberated by the pro-hormone converting enzyme." @default.
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- W2000657836 date "1988-01-01" @default.
- W2000657836 modified "2023-09-24" @default.
- W2000657836 title "Pro-opiomelanocortin and pro-vasopressin converting enzyme in pituitary secretory vesicles" @default.
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- W2000657836 doi "https://doi.org/10.1016/0300-9084(88)90153-8" @default.
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