Medical College of Wisconsin
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Involvement of an endogenous metalloprotease in the activation of protoxin in Bacillus thuringiensis subsp. kurstaki. Biochem Mol Biol Int 1997 Aug;42(5):901-8

Date

08/01/1997

Pubmed ID

9285057

DOI

10.1080/15216549700203341

Abstract

Insecticidal crystal proteins harvested from sporulated cultures of Bacillus thuringiensis subsp. kurstaki contain the protoxin (Mr 132 kDa) and minor amounts of toxin (66 kDa). The proteolytic processing of 132 kDa protoxin to an active 66 kDa toxin is brought about by exogenous proteases or larval gut enzymes. Under denaturing/reducing conditions this conversion is also mediated by endogenous protease(s) of the producer organism. This endogenous protease is identified as a metalloprotease as the activation process is inhibited by ethylenediamine tetraacetic acid at 2 mM concentration.

Author List

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
Insecticides
Metalloendopeptidases
Protein Precursors
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a