Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01275 (glucagon)
 26,492 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Atrial natriuretic peptide is rapidly degraded by a soluble, heat labile peptidase isolated from ventricular myocytes. Degradation of [125I]-ANP is antagonized by unlabelled ANP, bradykinin, glucagon, 1,10-phenanthroline, PCMB, EDTA and the bacterial antibiotic bacitracin, but not by phenylmethylsulphonyl fluoride, aprotinin, phosphoramidon, E-64, amastatin or the ACE inhibitor SQ 20881 and bradykinin potentiator C. In addition neither bovine serum albumin nor caesin afforded any protection against degradation. Peptidase activity was optimal at pH values above 8.5. The peptidase is likely to be of intracellular origin and may contribute to the extensive ANP degradative activity found in various ventricular muscle preparations.
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PMID:Degradation of [125I]-atrial natriuretic peptide by a soluble metallopeptidase isolated from rat ventricular myocytes. 296 71

Two distinct dipeptidyl aminopeptidases, which were designated DPP-A and DPP-B, were purified from soluble fraction of monkey brain using Leu-enkephalin as the substrate. The enzymes were purified 187 and 136 fold, respectively. Both enzymes showed the optimum pH in neutral range. Their molecular weights were almost equal and were estimated to be about 100,000. Their Km values with Leu-enkephalin as the substrate were 5.6 X 10(-5) and 1.1 X 10(-5) M, respectively. Among synthesized substrates, the highest affinity of the enzymes was toward arginyl-arginine beta-naphthylamide with the Km values of 6.25 X 10(-5) and 6.41 X 10(-5) M, respectively. Both enzyme activities were inhibited by the metal-chelators DFP and PCMB. Two hundred fifty microM arphamenine A inhibited DPP-A and -B with inhibition of 36.6% and 44.1%, respectively. Beta-endorphin, ACTH, and glucagon inhibited only DPP-B, while beta-lipotropin and angiotensin II inhibited both DPP-A and -B when Leu-enkephalin was used as the substrate.
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PMID:Purification and characterization of two distinct dipeptidyl aminopeptidases in soluble fraction from monkey brain and their action on enkephalins. 637 97