Naslov
New chloride-activated aminopeptidase from human erythrocytes

Autori
Abramić, Marija ; Vitale, Ljubinka

Izvornik
FEBS letters (0014-5793) 253 (1989), 1-2; 79-82

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

Ključne riječi
Aminopeptidase ; Alanyl aminopeptidase ; Halide activation ; Human erythrocytes

Sažetak
A new Cl--activated aminopeptidase was purified from the cytosol of human erythrocytes as a single chain protein of an approx. Mr, of 70 000 and pI of 5.1. The enzyme hydrolysed 2-naphthylamides of aliphatic, aromatic and basic L-amino acids, with a preference for the alanyl residue. It also hydrolysed di-, tri-, and some hydrophobic tetrapeptides. The inhibitors were bestatin, amastatin, Co2+, Zn2+, Mn2+, 4-hydroxymercuribenzoate and 1, 10-phenanthroline. The activity of the enzyme, inhibited by 4-hydroxymercuribenzoate, was partially restored by the addition of sulfhydryl compounds. The presence of 0.2 M Cl- (Br-, F-) caused a several-fold increase in the isolated aminopeptidase activity.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija

POVEZANOST RADA