Original scientific paper

Some Characteristics of Cathepsin Band a-N-Benzoylarginine- B-Naphthylamide Hydrolase From Bovine Lymph Nodes

T. Zvonar-Popovič ; Department of Biochemistry, J. Stefan Institute, 61000 Ljubljana, Yugoslavia
T. Lah ; Department of Biochemistry, J. Stefan Institute, 61000 Ljubljana, Yugoslavia
I. Kregar ; Department of Biochemistry, J. Stefan Institute, 61000 Ljubljana, Yugoslavia
V. Turk ; Department of Biochemistry, J. Stefan Institute, 61000 Ljubljana, Yugoslavia

Abstract

Some properties of cathepsin B and a-N-benzoylarginine-~-
naphthylamide (BANA) hydrolase from bovine lymph nodes have
been studies. a-N-benzoylarginine-~-naphthylamide was a sensitive
substrate for both enzymes. Leucine-2-naphthylamide was cleaved
only by BANA hydrolase. Degradation of low molecular weight
substrates was optimal at pH = 6.0. At this pH value, the enzymes
were most stable. Cathepsin B inactivated aldolase, was inhibited
by 1 μM leupeptin and by thiol blocking compounds. BANA hydrolase
was not inhibited by 1 μM leupeptin but showed that it required
thiol compounds and EDTA for full activation. It was concluded
that BANA hydrolase is very similar or identical to cathepsin
H from rat liver lysosomes.

Keywords

Hrčak ID:

194559

URI

https://hrcak.srce.hr/194559

Publication date:

15.11.1980.

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