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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Loh, Y. P. Gainer, H. |
| Abstract | Lysates of secretory granules from rat pituitary neurointermediate lobes were incubated with [3H]arginine- or [3H]phenylalanine-labeled toad pro-opiocortin. The processed products formed were identified by immunoprecipitation with adrenocorticotropin (ACTH) and endorphin antisera and by migration behavior on acid/urea/polyacrylamide gels. Pro-opiocortin was cleaved by the proteolytic activity in the secretory granule fraction to approximately 21,000 Mr ACTH, approximately 13,000 Mr ACTH, alpha-melanotropin, 16,000 Mr NH2-terminal glycopeptide, beta-lipotropin, and an endorphin-related peptide. Characterization of this pro-opiocortin-converting activity shows that it (i) is present in membrane and soluble fractions of the granule lysates, (ii) has a pH optimum of 5.0, (iii) appears to cleave at pairs of basic amino acid residues in the precursor, and (iv) is inhibited by leupeptin, pepstatin A, and p-chloromercuribenzoate but not diisopropyl fluorophosphate, N alpha-p-tosyl-L-lysine chloromethyl ketone hydrochloride, chloroquine, or EDTA. These inhibitor studies suggest that the converting-enzyme activity is due to an acid thiol, arginyl protease, distinct from any known cathepsin B-like activity. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 1 |
| Volume Number | 79 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1982-03-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adrenocorticotropic Hormone Metabolism Cytoplasmic Granules Enzymology Endopeptidases Pituitary Gland Pituitary Hormones, Anterior Protein Precursors Animals Isolation & Purification Kinetics Melanocyte-Stimulating Hormones Pro-Opiomelanocortin Proprotein Convertases Protease Inhibitors Pharmacology Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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