Affiliation:
1. Laboratory of Chemical Biology, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014
Abstract
The enzyme β-galactosidase was studied in crude extracts of
Escherichia coli
3300,
E. coli
grown on a selenium and sulfur medium,
Salmonella typhimurium
F-lac,
Serratia marcescens
F-lac,
S. marcescens
P-lac,
Proteus mirabilis
F-lac,
P. mirabilis
P-lac,
Aeromonas formicans
, and
Streptococcus lactis
. The isoenzymes could be demonstrated by an alternative histochemical technique. Different isoenzyme patterns were found to be determined by the β-galactosidase structural gene and not by the cytoplasm within which the β-galactosidase was formed. In addition, the β-galactosidases from strains which form isoenzymes were more stable to heat and urea treatments than the enzyme formed by those organisms which produce reduced amounts of, or no, isoenzyme.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
38 articles.
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