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New chloride-activated aminopeptidase from human erythrocytes (CROSBI ID 122476)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Abramić, Marija ; Vitale, Ljubinka New chloride-activated aminopeptidase from human erythrocytes // FEBS letters, 253 (1989), 1-2; 79-82. doi: 10.1016/0014-5793(89)80934-2

Podaci o odgovornosti

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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Podaci o izdanju

253 (1-2)

1989.

79-82

objavljeno

0014-5793

1873-3468

10.1016/0014-5793(89)80934-2

Povezanost rada

Biologija, Kemija

Poveznice
Indeksiranost