Synthetic peptides as substrates for processing enzymes in the bovine pituitary.
Synthetic peptides, based on sequences of proopiomelanocortin (POMC) cleaved in both the bovine anterior and intermediate pituitaries (-Phe-Pro-Leu-Gly-Phe-Lys-Arg-Glu-Leu-Thr-Gly-) and only in the intermediate lobe (-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-), were used as substrates for the enzymes that process POMC to active hormones in the anterior and intermediate lobes of the pituitary. Cleavage of these peptides at the dibasic pair of residues, the expected cleavage site, was observed with a lysate from bovine pituitary secretory granules. Cleavage occurred optimally at a pH between 4 and 5 and was inhibited with sulfhydryl reagents, pepstatin, and leupeptin. Little specificity for the nature of the basic residues at the cleavage site was observed. An additional cleavage, following glutamic acid residues, was also seen.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003594:Cytoplasmic Granules / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D010455:Peptides / Q000138:chemical synthesis; D010902:Pituitary Gland / Q000201:enzymology*; D011333:Pro-Opiomelanocortin / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D011499:Protein Processing, Post-Translational; D013329:Structure-Activity Relationship; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity
D010455:Peptides; D011480:Protease Inhibitors; D011333:Pro-Opiomelanocortin