Collect. Czech. Chem. Commun. 1985, 50, 1249-1257

Isolation and partial characterization of bovine liver aminopeptidase B

Ján Blahoveca, Michal Bartíka and Evžen Kasafírekb

a Department of Chemistry, Biochemistry, Toxicology and Pathological Physiology, School of Veterinary Medicine, 041 81 Košice
b Research Institute for Pharmacy and Biochemistry, 130 60 Prague 3


Aminopeptidase B, specifically hydrolyzing the L-lysine and L-arginine derivatives of p-nitroaniline and β-naphthylamine, was isolated from bovine liver. A multistep purification procedure involving fractionation with ammonium sulfate, gel filtration on Sephadex, ion exchange chromatography on Ecteola-cellulose, and adsorption chromatography on hydroxylapatite, afforded an enzyme whose activity was approximately 240 times higher than the activity of the original material. The molecular weight of the enzyme determined by gel filtration on Sephadex G-200 was approximately 55 000. The Michaelis constant with respect to L-lysyl-p-nitroanilide was 1.2 . 10-3 mol/l.