Basic Amino Acids Preferring Broad Specificity Aminopeptidase from Human Erythrocytes (CROSBI ID 122479)
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Podaci o odgovornosti
Abramić, Marija ; Vitale, Ljubinka
engleski
Basic Amino Acids Preferring Broad Specificity Aminopeptidase from Human Erythrocytes
An aminopeptidase hydrolyzing 2-naphthylamides of Lys, Arg, Leu, Met, Phe and Tyr, as well as different di- to tridecapeptides, was purified from the cytosol of human erythrocytes. The enzyme showed preference for Lys and Arg at N-terminus, as proline and D-amino acids were nonpermissive at P1' site. Higher affinity for oligopeptides than for aminoacyl naphthylamides was observed. Among the substrates were Lys-bradykinin, angiotensin III, thymopentin and enkephalins. Aminopeptidase was shown to be a monomeric protein of Mr approximately 110000 and of pI approximately 4.8, activated by Co2+ and inhibited by EDTA, pHMB, amastatin, bestatin and puromycin. The isolated enzyme could be classified as cytosolic, Lys(Arg) preferring, broad specificity aminopeptidase.
Broad specificity aminopeptidase ; Puromycin-sensitive aminopeptidase ; Human erythrocytes ; Erythrocyte enzyme
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Podaci o izdanju
373 (2)
1992.
375-380
objavljeno
0177-3593
10.1515/bchm3.1992.373.2.375