메뉴 건너뛰기




Volumn 31, Issue 9, 2001, Pages 909-918

Bacillus thuringiensis Cry1Ac and Cry1Fa δ-endotoxin binding to a novel 110 kDa aminopeptidase in Heliothis virescens is not N-acetylgalactosamine mediated

Author keywords

Endotoxin; Aminopeptidase; Bacillus thuringiensis; Binding protein; Cry1; Heliothis virescens; N acetylgalactosamine

Indexed keywords

AMINOPEPTIDASE; AMINOPEPTIDASE N, INSECT; BACILLUS THURINGIENSIS CRYSTAL PROTEIN; BACTERIAL PROTEIN; BIOTIN; CRY1AC ENDOTOXIN; CRY1FA SIGMA ENDOTOXIN; DODECYL SULFATE SODIUM; ENDOTOXIN; INSECT PROTEIN; IODINE 125; LECTIN; LIGAND; N ACETYLGALACTOSAMINE; PERIODATE; PERIODIC ACID; RADIOACTIVE IODINE; SOYBEAN AGGLUTININ; UNCLASSIFIED DRUG;

EID: 0035954588     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(01)00038-8     Document Type: Article
Times cited : (51)

References (35)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0028875319 scopus 로고
    • Identification, isolation, and cloning of a Bacillus thuringiensis Cry1Ac toxin-binding protein from the midgut of the lepidopteran insect Heliothis virescens
    • (1995) J. Biol. Chem. , vol.270 , pp. 27277-27282
    • Gill, S.S.1    Cowles, E.A.2    Francis, V.3
  • 17
    • 4244144005 scopus 로고
    • The crystal δ-endotoxin of Bacillus thuringiensis: Models for their mechanisms of action on the insect gut
    • (1993) Bioessays , vol.15 , pp. 469-476
    • Knowles, B.H.1    Dow, J.A.T.2
  • 22
    • 0032974991 scopus 로고    scopus 로고
    • Toxicity, binding and permeability analyses of four Bacillus thuringiensis Cry1 δ-endotoxins using brush border membrane vesicles of Spodoptera exigua and Spodoptera frugiperda
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 457-464
    • Luo, K.1    Banks, D.J.2    Adang, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.