Acylated Bovine Serum Albumin -- A New Substrate for Determining Cathepsin D Activity.
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.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 01, 1975
- Accession Number
- ADA018267
Entities
People
- D. C. White Jr.
- P. Z. Sobocinski
- S. L. Snyder
Organizations
- Armed Forces Radiobiology Research Institute