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
08/26/1998Pubmed ID
9713700DOI
10.1080/15216549800203182Scopus ID
2-s2.0-0344110514 (requires institutional sign-in at Scopus site) 4 CitationsAbstract
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 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
Amino Acid SequenceAnimals
Bacillus thuringiensis
Bacterial Proteins
Bacterial Toxins
Endopeptidases
Endotoxins
Hemolysin Proteins
Molecular Weight
Protein Precursors
Protein Processing, Post-Translational
Spodoptera