Naslov
Basic Amino Acids Preferring Broad Specificity Aminopeptidase from Human Erythrocytes

Autori
Abramić, Marija ; Vitale, Ljubinka

Izvornik
Biological Chemistry Hoppe-Seyler (0177-3593) 373 (1992), 2; 375-380

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Broad specificity aminopeptidase ; Puromycin-sensitive aminopeptidase ; Human erythrocytes ; Erythrocyte enzyme

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija

POVEZANOST RADA