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Endocrinology, Vol 111, 1607-1614, Copyright © 1982 by Endocrine Society

ARTICLES

Proopiocortin-converting enzyme activity in bovine neurosecretory granules

TL Chang, H Gainer, JT Russell and YP Loh

Neurosecretory granules (NSGs) from neural lobes of bovine pituitary glands were isolated in a highly purified form by metrizamide-sucrose gradient centrifugation. The purified NSGs were lysed and centrifuged, and the supernatants were further fractionated by gel filtration on Sephadex G-75. Proopiocortin-converting enzyme activity was assayed by incubation of [3H]arginine- or [3H]phenylalanine-labeled toad proopiocortin with NSG supernatant fractions. The processed products were identified by immunoprecipitation with ACTH and beta-endorphin antisera, followed by acid-urea gel electrophoresis. The optimum pH for the enzyme-mediated conversion was around pH 5.0. Conversion of toad proopiocortin by NSG converting enzyme activity was inhibited by leupeptin, antipain, p-chloromercuribenzoate, and pepstatin A, but not by diisopropyl fluorophosphate, EDTA, or N-alpha-p-tosyl-L-lysine- chloromethyl ketone HCl. The results suggest that the proopiocortin- converting enzyme activity in bovine neurosecretory granules is due to an acid-thiol protease which may contain secondary hydrophobic binding sites that are involved in substrate recognition.


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M. Whitnall, H Gainer, B. Cox, and C. Molineaux
Dynorphin-A-(1-8) is contained within vasopressin neurosecretory vesicles in rat pituitary
Science, December 9, 1983; 222(4628): 1137 - 1139.
[Abstract] [PDF]


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