Tags

Type your tag names separated by a space and hit enter

Luminal proteinases from Plodia interpunctella and the hydrolysis of Bacillus thuringiensis CryIA(c) protoxin.
Insect Biochem Mol Biol. 1996 Jun; 26(6):571-83.IB

Abstract

The ability of proteinases in gut extracts of the Indianmeal moth, Plodia interpunctella, to hydrolyze Bacillus thuringiensis (Bt) protoxin, casein, and rho-nitroanilide substrates was investigated. A polyclonal antiserum to protoxin CryIA(c) was used in Western blots to demonstrate slower protoxin processing by gut enzymes from Bt subspecies entomocidus-resistant larvae than enzymes from susceptible or kurstaki-resistant strains. Enzymes from all three strains hydrolyzed N-alpha-benzoyl-L-arginine rho-nitroanilide, N-succinyl-ala-ala-pro-phenylalanine rho-nitroanilide, and N-succinyl-ala-ala-pro-leucine rho-nitroanilide. Zymograms and activity blots were used to estimate the apparent molecular masses, number of enzymes, and relative activities in each strain. Several serine proteinase inhibitors reduced gut enzyme activities, with two soybean trypsin inhibitors, two potato inhibitors, and chymostatin the most effective in preventing protoxin hydrolysis.

Authors+Show Affiliations

U.S. Grain Marketing Research Laboratory, ARS-USDA, Manhattan, KS 66502-2736, USA. bso@ksu.ksu.eduNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

8969468

Citation

Oppert, B, et al. "Luminal Proteinases From Plodia Interpunctella and the Hydrolysis of Bacillus Thuringiensis CryIA(c) Protoxin." Insect Biochemistry and Molecular Biology, vol. 26, no. 6, 1996, pp. 571-83.
Oppert B, Kramer KJ, Johnson D, et al. Luminal proteinases from Plodia interpunctella and the hydrolysis of Bacillus thuringiensis CryIA(c) protoxin. Insect Biochem Mol Biol. 1996;26(6):571-83.
Oppert, B., Kramer, K. J., Johnson, D., Upton, S. J., & Mcgaughey, W. H. (1996). Luminal proteinases from Plodia interpunctella and the hydrolysis of Bacillus thuringiensis CryIA(c) protoxin. Insect Biochemistry and Molecular Biology, 26(6), 571-83.
Oppert B, et al. Luminal Proteinases From Plodia Interpunctella and the Hydrolysis of Bacillus Thuringiensis CryIA(c) Protoxin. Insect Biochem Mol Biol. 1996;26(6):571-83. PubMed PMID: 8969468.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Luminal proteinases from Plodia interpunctella and the hydrolysis of Bacillus thuringiensis CryIA(c) protoxin. AU - Oppert,B, AU - Kramer,K J, AU - Johnson,D, AU - Upton,S J, AU - Mcgaughey,W H, PY - 1996/6/1/pubmed PY - 2000/3/23/medline PY - 1996/6/1/entrez SP - 571 EP - 83 JF - Insect biochemistry and molecular biology JO - Insect Biochem Mol Biol VL - 26 IS - 6 N2 - The ability of proteinases in gut extracts of the Indianmeal moth, Plodia interpunctella, to hydrolyze Bacillus thuringiensis (Bt) protoxin, casein, and rho-nitroanilide substrates was investigated. A polyclonal antiserum to protoxin CryIA(c) was used in Western blots to demonstrate slower protoxin processing by gut enzymes from Bt subspecies entomocidus-resistant larvae than enzymes from susceptible or kurstaki-resistant strains. Enzymes from all three strains hydrolyzed N-alpha-benzoyl-L-arginine rho-nitroanilide, N-succinyl-ala-ala-pro-phenylalanine rho-nitroanilide, and N-succinyl-ala-ala-pro-leucine rho-nitroanilide. Zymograms and activity blots were used to estimate the apparent molecular masses, number of enzymes, and relative activities in each strain. Several serine proteinase inhibitors reduced gut enzyme activities, with two soybean trypsin inhibitors, two potato inhibitors, and chymostatin the most effective in preventing protoxin hydrolysis. SN - 0965-1748 UR - https://www.unboundmedicine.com/medline/citation/8969468/Luminal_proteinases_from_Plodia_interpunctella_and_the_hydrolysis_of_Bacillus_thuringiensis_CryIA_c__protoxin_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0965174896000136 DB - PRIME DP - Unbound Medicine ER -