Tags

Type your tag names separated by a space and hit enter

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.BM

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.

Authors+Show Affiliations

Kumar NS
Department of Biochemistry, Osmania University, Hyderabad, India.
Venkateswerlu G
No affiliation info available

MeSH

Amino Acid SequenceAnimalsBacillus thuringiensisBacillus thuringiensis ToxinsBacterial ProteinsBacterial ToxinsEndopeptidasesEndotoxinsHemolysin ProteinsMolecular WeightProtein PrecursorsProtein Processing, Post-TranslationalSpodoptera

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9713700

Citation

Kumar, N S., and G Venkateswerlu. "Analysis of 66 kDa Toxin From Bacillus Thuringiensis Subsp. Kurstaki Reveals Differential Amino Terminal Processing of Protoxin By Endogenous Protease(s)." Biochemistry and Molecular Biology International, vol. 45, no. 4, 1998, pp. 769-74.
Kumar NS, Venkateswerlu G. 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;45(4):769-74.
Kumar, N. S., & Venkateswerlu, G. (1998). Analysis of 66 kDa toxin from Bacillus thuringiensis subsp. kurstaki reveals differential amino terminal processing of protoxin by endogenous protease(s). Biochemistry and Molecular Biology International, 45(4), 769-74.
Kumar NS, Venkateswerlu G. 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;45(4):769-74. PubMed PMID: 9713700.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Analysis of 66 kDa toxin from Bacillus thuringiensis subsp. kurstaki reveals differential amino terminal processing of protoxin by endogenous protease(s). AU - Kumar,N S, AU - Venkateswerlu,G, PY - 1998/8/26/pubmed PY - 1998/8/26/medline PY - 1998/8/26/entrez SP - 769 EP - 74 JF - Biochemistry and molecular biology international JO - Biochem Mol Biol Int VL - 45 IS - 4 N2 - 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. SN - 1039-9712 UR - https://www.unboundmedicine.com/medline/citation/9713700/Analysis_of_66_kDa_toxin_from_Bacillus_thuringiensis_subsp__kurstaki_reveals_differential_amino_terminal_processing_of_protoxin_by_endogenous_protease_s__ DB - PRIME DP - Unbound Medicine ER -