Accession Number : ADA018267

Title :   Acylated Bovine Serum Albumin -- A New Substrate for Determining Cathepsin D Activity.

Descriptive Note : Technical note,

Corporate Author : ARMED FORCES RADIOBIOLOGY RESEARCH INST BETHESDA MD

Personal Author(s) : Snyder,S. L. ; White,D. C. , Jr. ; Sobocinski,P. Z.

Report Date : AUG 1975

Pagination or Media Count : 18

Abstract : Partially purified cathepsin D obtained from bovine uterus catalyzes the proteolysis of acylated bovine serum albumin (Ac-BSA). A sensitive method for measuring cathepsin D activity based on the use of Ac-BSA as the substrate is reported. In addition, the effect of pH and substrate concentration on the rate of proteolysis has been studied. The apparent Michaelis constant (Km) at pH 3.2 for the cathepsin D Ac-BSA complex was evaluated as 3.1 mg/ml.

Descriptors :   *Serum albumin, *Enzymes, Proteins, Bovines, Chemical properties, Measurement, pH factor, Substrates

Subject Categories : Biochemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE