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Transcriptome‐based phylogeny of endemic Lake Baikal amphipod species flock: fast speciation accompanied by frequent episodes of positive selection 下载免费PDF全文
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G. G. Chestukhina L. I. Kostina A. L. Mikhailova S. A. Tyurin F. S. Klepikova V. M. Stepanov 《Archives of microbiology》1982,132(2):159-162
The crystal-forming proteins (-endotoxins) produced by various serotypes of Bacillus thuringiensis and toxic for Lepidoptera reveal the same pattern of molecular organisation. These proteins (M
r of ca. 145,000–130,000) contain an N-terminal domain (M
r of 85,000–65,000) resistant to proteolysis whereas their C-terminal moieties (M
r of 65,000) undergo an extensive degradation by trypsin that leads to stepwise cleavage off the fragments with M
r of 15,000–35,000.The N-terminal domain from serotype V -endotoxin is active when introduced into the hemocoel of Galleria mellonella larvae. Hence, it correponds to the true toxin normally formed by larva proteases action on the crystalforming protein (protoxin). Some differences were found in the properties of the N-terminal domains isolated from the crystal-forming proteins of III, V and IX serotypes, e.g., in their solubility, digestion by subtilisin, molecular weights and the distribution of methionine residues along the polypeptide chains.Abbreviations SDS
sodium dodecyl sulphate
- PAGE
polyacryl amide gel electrophoresis
- CFP
crystal-forming protein
- DNS
5-dimethylamino-1-naphthalene-sulphonyl 相似文献
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G.G. Chestukhina I.A. Zalunin L.I. Kostina M.E. Bormatova F.S. Klepikova O.M. Khodova V.M. Stepanov 《FEBS letters》1985,190(2)
Entomocidal crystals produced by Bacillus thuringiensis ssp. israelensis are formed by two proteins with molecular masses of 130 and 28 kDa, whereas the protein with a molecular mass of 70 kDa appears as a result of 130 kDa protein limited proteolysis by admixtures of bacterial proteinases in the course of its dissolution. The comparison of the N-terminal sequences of the protein with molecular mass of 70 kDa (Met-Glu-Asn-Xaa-Pro-Leu-Asp-Thr-Leu-Ser-Ile-Val-Asn-Glu-Thr-Asp) and that of 28 kDa (Met-Glu-Asn-Leu-Asn-[Phe]-[Trp]-Pro-Leu-Gln-Asp-Ile-Lys-Val-Asn-Pro) reveals only marginal similarity between them (only 4 identical residues among 16 aligned). Both B. thuringiensis israelensis crystal-forming proteins appear hardly related to those contained in the crystal produced by other B. thuringiensis subspecies, e.g. kurstaki. It might be concluded that at least some of the entomocidal proteins found in the crystalline inclusion bodies of various B. thuringiensis subspecies revealed rather strong variations in their primary structures that facilitate their adaptation to different hosts.Bacillus thuringiensis ssp. israelensis δ-EndotoxinEntomocidal crystalInsecticideMosquito 相似文献
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Virulent and temperate bacterial phages were isolated from the cultural broth of Bacillus licheniformis obtained under the industrial conditions when synthesis of the antibiotic bacitracin was interfered with. The following properties of the phages were studied: the fine structure, the morphology of negative colonies, the spectrum of lytic action, the rate of adsorption, the individual growth cycle, as well as the lysogenic state of certain strains of Bac. licheniformis. Some phages were serologically related and morphologically identical whereas others differed sharply in their morphology and antigenic properties. 相似文献