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Analysis of 66 kDa toxin from Bacillus thuringiensis subsp. kurstaki reveals differential amino terminal processing of protoxin by endogenous protease(s). Biochem Mol Biol Int 1998 Jul;45(4):769-74

Date

08/26/1998

Pubmed ID

9713700

DOI

10.1080/15216549800203182

Abstract

The endogenous protease(s) activated crystal toxin from Bacillus thuringiensis subsp. kurstaki was purified and examined. The purified toxin was homogenous, as demonstrated by two-dimensional polyacrylamide gel electrophoresis and contained 1.38 mumoles neutral sugar and 9 nmoles sialic acid per mg protein amino terminal amino acid sequence data revealed that the toxin is a cleavage product of 132 kDa protoxin with glutamic acid-30 of the deduced amino acid sequence of the crystal protein (Schnepf, H.E., Wong, H.C. and Whiteley, H.R. (1985) J. Biol. Chem. 260: 6264-6272) at the amino terminus.

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

Amino Acid Sequence
Animals
Bacillus thuringiensis
Bacterial Proteins
Bacterial Toxins
Endopeptidases
Endotoxins
Hemolysin Proteins
Molecular Weight
Protein Precursors
Protein Processing, Post-Translational
Spodoptera
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a