sodium-dodecyl-sulfate has been researched along with 4-toluenesulfonyl-fluoride* in 2 studies
2 other study(ies) available for sodium-dodecyl-sulfate and 4-toluenesulfonyl-fluoride
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Properties and application of a partially purified alkaline xylanase from an alkalophilic fungus Aspergillus nidulans KK-99.
An alkalophilic Aspergillus nidulans KK-99 produced an alkaline, thermostable xylanase (40 IU/ml) in a basal medium supplemented with wheat bran (2% w/v) and KNO3 (at 0.15% N) pH 10.0 and 37 degrees C. The partially purified xylanase was optimally active at pH 8.0 and 55 degrees C. The xylanase was stable in a broad pH range of 4.0-9.5 for 1 h at 55 degrees C, retaining more than 80% of its activity. The enzyme exhibited greater binding affinity for xylan from hardwood than from softwood. The xylanase activity was stimulated (+25%) by Na+ and Fe2+ and was strongly inhibited (maximum by 70%) by Tween-20, 40, 60, SDS, acetic anhydride, phenylmethane sulphonyl fluoride, Triton-X-100. The xylanase dose of 1.0 IU/g dry weight pulp gave optimum bleach boosting of Kraft pulp at pH 8.0 and temperature 55 degrees C for 3 h reaction time. Topics: Acetic Anhydrides; Aspergillus nidulans; Chlorine Compounds; Culture Media; Enzyme Activation; Enzyme Stability; Hydrogen-Ion Concentration; Industrial Microbiology; Industry; Iron; Nitrates; Paper; Photobleaching; Polysorbates; Potassium Compounds; Protease Inhibitors; Sodium; Sodium Dodecyl Sulfate; Streptomyces; Substrate Specificity; Surface-Active Agents; Temperature; Time Factors; Tosyl Compounds; Triticum; Xylan Endo-1,3-beta-Xylosidase; Xylans; Xylosidases | 2002 |
Adherence of Borrelia burgdorferi to granulocytes of different animal species.
Adherence of 4 Borrelia (B.) burgdorferi strains (z7/22, z7/27, z7/41, PBi) to polymorphonuclear granulocytes from different domestic animals (horses, cattle, sheep, dogs) was investigated. All 4 strains adhered to the granulocytes. Binding assays indicated that the adherence occurred between structures on the surface of the borreliae ("binding-sites") and on the membranes of the granulocytes ("receptors"). The "receptors" consisted of 4 fractions (A, B, C, and D) with components differing in molecular weight (MW) and binding activity for proteins on the surface of B. burgdorferi. Fraction A (MW 80000) had the highest binding activity for B. burgdorferi. Topics: Animals; Bacterial Adhesion; Borrelia burgdorferi Group; Cattle; Cells, Cultured; Detergents; Dogs; Granulocytes; Heating; Horses; Humans; Octoxynol; Receptors, Cell Surface; Sheep; Sodium Dodecyl Sulfate; Tosyl Compounds | 1997 |