Acid proteinase of chicken liver. Purification and properties

F. Barceló
N. Vives
J. Bozal
45

Abstract

A method for purifying the haemoglobinolitic activity to acid pH in chicken liver is described.The purified preparation contains cathespin D activity since it is inhibited by diazoacetyl-DL-norleucine methylester in the presence of cupric ions, while thiol-enzyme reagents do not affect it.The molecular weight of the enzyme is approximately 40,000–45,000 and the pH optimum against haemoglobin and bovine serum albumin is 3.5-03.7.The rate of degradation of albumin and casein is much less than that of haemoglobin.Cathepsin D preparations with different purification degrees, exhibit a similar percentage of activation at acid pH; the highest activation is observed at pH 3.1-03.3.

Keywords:
Animals, Chickens/metabolism, Hydrogen-Ion Concentration, Liver/enzymology, Peptide Hydrolases/isolation and purification

Authors

F. Barceló
N. Vives
J. Bozal


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