Accession Number : AD0703180

Title :   ISOLATION AND INITIAL STUDIES ON A PROTEINASE FROM HUMAN ERYTHROCYTE MEMBRANES.

Descriptive Note : Interim rept.,

Corporate Author : ARMY MEDICAL RESEARCH LAB FORT KNOX KY

Personal Author(s) : Moore,Gerald L. ; Kocholaty,Walter F. ; Cooper,Donald A. ; Gray,John L. ; Robinson,Stephen L.

Report Date : 09 DEC 1969

Pagination or Media Count : 23

Abstract : An enzyme was isolated from human erythrocyte membranes with proteolytic activity toward casein, hemoglobin, stroma proteins, and certain synthetic substrates. This enzyme may be extracted from membranes by a number of 1 M salt solutions and stored either at 4C or frozen for several weeks. A standard assay procedure using Azocoll is defined for this proteinase. Activation is shown to occur when the proteinase is treated with solutions of KCNS. Initial purification by column chromatography gives a protein fraction with most of the proteolytic activity in 20% of the total extracted protein. This protein fraction contains three to five species by disc electrophoresis, one or two of which have the proteolytic activity. Experiments with the ultracentrifuge indicate that the proteolytic activity is a part of, or is bound to, one or more lipoprotein species. This proteinase has the potential of acting as an important step in the chain of events that occur during erythrocyte hemolysis. (Author)

Descriptors :   (*ERYTHROCYTES, MEMBRANES(BIOLOGY)), (*MEMBRANES(BIOLOGY), PEPTIDE HYDROLASES), (*PEPTIDE HYDROLASES, ERYTHROCYTES), HEMOGLOBIN, CASEIN, PROTEINS, ENZYMES, CHROMATOGRAPHIC ANALYSIS, PURIFICATION, ELECTROPHORESIS, CENTRIFUGE SEPARATION, HEMOLYSIS, LIPOPROTEINS, CHEMICAL ANALYSIS, BLOOD

Subject Categories : Biochemistry
      Anatomy and Physiology

Distribution Statement : APPROVED FOR PUBLIC RELEASE