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
08/01/1997Pubmed ID
9285057DOI
10.1080/15216549700203341Scopus ID
2-s2.0-0344541099 (requires institutional sign-in at Scopus site) 12 CitationsAbstract
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 GAuthor
Suresh Kumar PhD Associate Professor in the Pathology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Bacillus thuringiensisBacterial Proteins
Bacterial Toxins
Insecticides
Metalloendopeptidases
Protein Precursors