Effects of Halides on Dipeptidyl and Tripeptidyl Carboxypeptidase Activities of Kininase II
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The effects of halides on the dipeptidyl and tripeptidyl carboxypeptidase activities of kininase II (angiotensin-converting enzyme, EC 3.4.15.1) purified from hog kidney were investigated. The dipeptidyl carboxypeptidase activity of the enzyme for bradykinin in the absence of halides was found to be buffer-dependent, and was decreased by the anions in potassium phosphate, N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid (Hepes), Tris-H_2SO_4,Tris-H_3PO_4 and Trisacetate buffers with increasing concentration of these buffers (1-100mM) ; however, the activity was unaffected by borate-sodium carbonate buffer in this concentration range. When boratesodium carbonate buffer was used, F^- functioned as an activator by raising V (2-fold) without modifying K_m, while the other halides (Cl^-, Br^- and I^-) hardly influenced V/K_m (there were decreases of both V and K_m), despite the fact that all the halides functioned as activators in various buffers by raising V (maximum 14-fold) without markedly affecting K_m when angiotensin I was the substrate. The stimulatory effect of F^- on bradykinin hydrolytic activity was maximum at 10mM, and it was reversed by various other anions (Cl^-, Br^-, I^-, PO^<3->_4,SO^<2->_4,Hepes and CH_3COO^-). The V value of the enzyme for Gly-Phe-Ser-Pro-Phe (des-Arg^9-bradykinin analogue), which is a substrate for the tripeptidyl carboxypeptidase activity of the enzyme (Biochim. Biophys. Acta, 662,300,1981), was enhanced by the addition of halides in the order Cl^->Br^->I^->F^-. On the other hand, the V value of the tripeptidyl carboxypeptidase activity of the enzyme for Gly-Pro-Ser-Pro-Phe, which has a proline residue at P_1,like bradykinin, was enhanced to a lesser degree by halides and the maximal activity was obtained by the addition of 100mM F^- (which resulted in a 2-fold increase of V).
- 社団法人日本薬学会の論文
- 1984-01-25
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