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Basic Amino Acids Preferring Broad Specificity Aminopeptidase from Human Erythrocytes (CROSBI ID 122479)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Abramić, Marija ; Vitale, Ljubinka Basic Amino Acids Preferring Broad Specificity Aminopeptidase from Human Erythrocytes // Biological Chemistry Hoppe-Seyler, 373 (1992), 2; 375-380. doi: 10.1515/bchm3.1992.373.2.375

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

Povezanost rada

Kemija, Biologija

Poveznice
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