Affiliation:
1. Department of Bacteriology, University of California, Los Angeles, California 90024
Abstract
The crystalline inclusion of
Bacillus thuringiensis
, dissolved in 8
m
urea containing 10% 2-mercaptoethanol and dialyzed to
p
H 8.3 to 8.5, was compared with a fraction obtained by the same extraction procedure from spores broken by dry rupture. The two fractions behaved similarly on chromatography with Sephadex G-100 and diethylaminoethyl cellulose. The preparations behaved identically on acrylamide gel electrophoresis at
p
H 12 and
p
H 9.5. Further, peptide maps of the two fractions obtained after digestion with trypsin were almost superimposable. Amino acid analyses of the crystal and spore fraction were closely similar; discrepancies are attributed to contamination of the spore extract with small amounts of other proteins. It is concluded that a significant portion of the spore protein is identical with the crystal protein.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
51 articles.
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