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26 results for “SDS-PAGE”
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Research ArticleOpen accessIn the abstractTransgenic Indian Cotton (Gossypium hirsutum) Harboring Rice Chitinase Gene (Chi II) Confers Resistance to Two Fungal PathogensM. Ganesan, P. Bhanumathi, K. Ganesh Kumari et al.Problem statement: The present investigation described a simple and reproducible protocol for transgenic cotton regeneration and characterization of chitinase (Chi II) gene expression against two different fungal pathogens in cotton. Approach: Transgenic cotton (Gossypium hirsutum cv. SVPR2) plants were produced by pCambia-bar-Chi II (13.8 kb) under the control of the CaMV 35S promoter, harbored in the strain LBA 4404 Agrobacterium … …American Journal of Biochemistry and Biotechnology, Vol. 5, Issue 2 · 30 Jun 2009 · 8,531 accessesView PDFCite
Research ArticleOpen accessIn the abstractInfluence of the Prostatic Fluid from the First and Third Fractions of the Ejaculates on the Cryosurvival of Poodle Dog SpermHideaki Yamashiro, Kaori Narita, Satoshi Sugimura et al.Problem statement: Two experiments were conducted to determine the effect of the prostatic fluid from the first and third fractions of the ejaculates on the freezability of poodle dog sperm. Approach: The ejaculates from 2 trained poodle dogs were collected. Effect of prostatic fluid from the first and third fractions of ejaculates on cryosurvival of dog sperm was examined. SDS-PAGE … …American Journal of Animal and Veterinary Sciences, Vol. 4, Issue 1 · 31 Mar 2009 · 7,831 accessesView PDFCite
Research ArticleOpen accessIn the abstractA Putative Serine protease from Larval Midgut of Red Palm Weevil Rhynchophorus ferrugineus (Olivier) (Coleoptera: Curculionidae): Partial Purification and Biochemical CharacterizationAhmed Al Jabr, Mahmoud Abo-El-SaadA putative serine protease was isolated and partially purified from larval midgut of red palm weevil (RPW), Rhynchophorus ferrugineus (Olivier) using anion exchange chromatography, DE-52. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of this protease showed that the major band has a molecular weight of approximately 24 kDa corresponding to the same molecular weight of mammalian trypsin. In addition, zymography … …American Journal of Environmental Sciences, Vol. 4, Issue 6 · 31 Dec 2008 · 7,018 accessesView PDFCite
Research ArticleOpen accessIn the abstractProtective Effects of Covalent Cross-Linking on Proteolysis of Human Coproporphyrinogen Oxidase and Implications for PorphyriaAhmed W. Jafri, Jason R. Stephenson, Justin B. Morgenthaler et al.The effects of covalent cross-linkers on the enzyme, coproporphyrinogen oxidase, had been previously studied but their role in protecting the enzyme from protease cleavage has not been evaluated. Therefore, we examined how the cross-linker bis (sulfosuccinimidyl) suberate (BS3) affects the ability of trypsin to digest purified, wild type recombinant human coproporphyrinogen oxidase and selected mutants. Following incubation, the apparent molecular … …American Journal of Biochemistry and Biotechnology, Vol. 4, Issue 4 · 31 Dec 2008 · 6,687 accessesView PDFCite
Research ArticleOpen accessIn the abstractMolecular Characterization of Soybean Mosaic Virus NIa Protein and its Processing Event in Bacterial ExpressionBong K. Choi, Jae S. Park, Hye J. Ahn et al.Soybean mosaic virus (SMV)-CN18 is an Rsv resistance-breaking (RB) isolate to overcome soybean resistance genes Rsv1, Rsv3 and Rsv4. The aim of this study was to characterize nuclear inclusion protein a (NIa protein) of RB isolate at the molecular level and demonstrate its processing into genome-linked protein (VPg) and NIa-Pro domains in Esherichia coli containing a bacterial expression pET vector … …American Journal of Biochemistry and Biotechnology, Vol. 2, Issue 4 · 31 Dec 2006 · 6,902 accessesView PDFCite
Research ArticleOpen accessIn the abstractUse of Cross-linking to Assess Subunit Interaction of Recombinant Human Coproporphyrinogen OxidaseJason R. Stephenson, Nancy E. Thomas, Jon A. Friesen, Marjorie A. JonesTo provide further evidence for a dimeric form of coproporphyrinogen oxidase reported using the conventional hydrodynamic methods, bifunctional cross-linkers were incubated with purified, recombinant human coproporphyrinogen oxidase to determine subunit interaction in solution. The use of cross-linkers provides an effective way to demonstrate subunit association and allows for assessment of activity upon covalent cross-linking. Following incubation with selected cross-linkers, enzyme … …American Journal of Biochemistry and Biotechnology, Vol. 1, Issue 2 · 30 Jun 2005 · 6,594 accessesView PDFCite