FEBS Letters | |
Rabbit fast skeletal muscle phospholipase C Molecular weight determination by renaturation after polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate | |
Heilmeyer, Ludwig M.G.1  Windhofer, Volker1  Varsànyi, Magdolna1  | |
[1] Institut für Physiologische Chemie, Abteilung für Biochemie Supramolekularer Systeme, Ruhr-Universität Bochum, Universitätsstr. 150, 4630 Bochum I, Germany | |
关键词: Phospholipase C; Fast skeletal muscle; Molecular weight determination; Renaturation; Ins(1; 4; 5)P3; d-myo-inositol 1; 4; 5-triphosphate; PtdIns; 1-(3-sn-phosphatidyl)-1d-myo-inositol; PtdIns(4)P; 1-(3-sn-phosphatidyl)-1d-myo-inositol-4-phospahte; PtdIns(4; 5)P2; 1-(3-sn-phosphatidyl)-1d-myo-inositol-4; 5-bisphosphate; PtdSer; (3-sn-phosphatidyl)2; serine; PtdFln; (3-sn-phosphatidyl)ethanolamine; DOC; deoxycholate; SDS; sodium dodecylsulfate; | |
DOI : 10.1016/0014-5793(92)81182-L | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Phosphoinositide specific phospholipase C from rabbit fast skeletal muscle has been enriched ca. 1,000-fold with a specific activity of 40 μmol × min−1 × mg−1. Following SDS-PAGE, renaturation of the enzyme protein in the presence of deoxycholate allowed the determination of an apparent molecular weight of 110 kDa. Gel-filtration of the native enzyme resulted in a very similar apparent molecular weight of 115 kDa, however, associated proteins of higher molecular weight were also found. Free Ca2+ concentrations needed for half-maximal activation of PtdIns(4,5)P2, PtdIns4P and PtdIns hydrolysis are 6.3 μM, 85 μM and 1.8 mM, and the Km values for these substrates 102, 340 and 937 μM, respectively.
【 授权许可】
Unknown
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