Accession Number : AD0722288

Title :   Urease: Two Active Forms,

Corporate Author : NATIONAL RESEARCH COUNCIL OF CANADA OTTAWA (ONTARIO) DIV OF BIOLOGY

Personal Author(s) : Lynn,K. R.

Report Date : 15 JUL 1970

Pagination or Media Count : 6

Abstract : On DEAE-Sephadex, urease was separated into two active components. These were each of molecular weight 483,000 and had identical amino acid compositions. The observed nature of the fractionation, together with these results suggest isolation of conformeric isoenzymes of urease. (Author)

Descriptors :   (*UREASE, CHROMATOGRAPHIC ANALYSIS), (*ENZYMES, CHROMATOGRAPHIC ANALYSIS), AMIDE HYDROLASES, CHEMICAL ANALYSIS, CENTRIFUGE SEPARATION, PROTEINS, AMINO ACIDS, CHEMICAL PROPERTIES, CANADA

Subject Categories : Biochemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE