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Identification and purification of the 69-kDa intracellular protease involved in the proteolytic processing of the crystal delta-endotoxin of Bacillus thuringiensis subsp. tenebrionis. FEMS Microbiol Lett 2000 Feb 01;183(1):63-6

Date

01/29/2000

Pubmed ID

10650203

DOI

10.1111/j.1574-6968.2000.tb08934.x

Abstract

The dynamics of appearance of intracellular proteases in relation to the synthesis of crystal delta-endotoxin was studied to identify the native intracellular protease(s) involved in the proteolytic processing of the 73-kDa protoxin of Bacillus thuringiensis subsp. tenebrionis. In vitro proteolytic activation of the 73-kDa protoxin indicated the possible role of 69-kDa protease in the proteolytic processing of 73-kDa protoxin. The purified 69-kDa protease was able to cause the proteolytic activation of the 73-kDa protoxin to 68-kDa toxin and this conversion was inhibited by ethylenediamine tetraacetic acid and 1,10-phenanthroline.

Author List

Reddy ST, Kumar NS, Venkateswerlu G

Author

Suresh Kumar PhD Associate Professor in the Pathology department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Bacillus thuringiensis
Bacterial Proteins
Bacterial Toxins
Electrophoresis, Polyacrylamide Gel
Endopeptidases
Endotoxins
Hemolysin Proteins
Humans
Immunoblotting
Metalloendopeptidases
Protease Inhibitors
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