Skórko R, Osipiuk J, Stetter K O
Lehrstuhl für Mikrobiologie, Universität Regensburg, Federal Republic of Germany.
J Bacteriol. 1989 Sep;171(9):5162-4. doi: 10.1128/jb.171.9.5162-5164.1989.
Glycogen-bound polyphosphate kinase has been isolated from a crude extract of Sulfolobus acidocaldarius by isopycnic centrifugation in CsCl. Divalent cations (Mn2+ greater than Mg2+) stimulated the reaction. The enzyme does not require the presence of histones for its activity; it is inhibited strongly by phosphate and slightly by fluoride. The protein from the glycogen complex migrated in a sodium dodecyl sulfate-polyacrylamide gel as a 57-kilodalton protein band; after isoelectric focusing it separated into several spots in the pH range of 5.6 to 6.7.
通过在氯化铯中进行等密度离心,从嗜酸热硫化叶菌的粗提物中分离出了与糖原结合的多聚磷酸激酶。二价阳离子(锰离子比镁离子更有效)能刺激该反应。该酶的活性不需要组蛋白的存在;它受到磷酸盐的强烈抑制,受到氟化物的轻微抑制。糖原复合物中的蛋白质在十二烷基硫酸钠-聚丙烯酰胺凝胶中迁移时呈现为一条57千道尔顿的蛋白带;等电聚焦后,它在5.6至6.7的pH范围内分离成几个斑点。