New chloride-activated aminopeptidase from human erythrocytes (CROSBI ID 122476)
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Abramić, Marija ; Vitale, Ljubinka
engleski
New chloride-activated aminopeptidase from human erythrocytes
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.
Aminopeptidase ; Alanyl aminopeptidase ; Halide activation ; Human erythrocytes
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