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亲和层析纯化肌质网Ca2+-ATP酶
引用本文:屠亚平,徐红.亲和层析纯化肌质网Ca2+-ATP酶[J].生物化学与生物物理进展,1995,22(4):345-349.
作者姓名:屠亚平  徐红
作者单位:中国科学院生物物理研究所生物大分子国家重点实验室;中国科学院生物物理研究所生物大分子国家重点实验室
摘    要:建立了一种亲和层析纯化肌质网Ca2+-ATP酶的方法.用非离子型去污剂C12E8 溶解肌质网,再通过反应红-120琼脂糖亲和层析柱使肌质网Ca2+-ATP酶纯度从粗品中的65%提高到99%,并具有较高ATP水解活性.经SDS-聚丙烯酰胺凝胶电泳检测,为电泳纯.

关 键 词:肌质网Ca2+-ATP酶    反应红-120琼脂糖    亲和层析
收稿时间:1995/1/12 0:00:00
修稿时间:1995/2/15 0:00:00

Purification of Ca2+-ATPase from Sarcoplasmic Reticulum by Affinity Gel Chromatography
Tu Yaping and Xu Hong.Purification of Ca2+-ATPase from Sarcoplasmic Reticulum by Affinity Gel Chromatography[J].Progress In Biochemistry and Biophysics,1995,22(4):345-349.
Authors:Tu Yaping and Xu Hong
Institution:National Key Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica;National Key Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica
Abstract:Ca2+-ATPase from rabbit skeletal muscle sarcoplasmic reticulum vesicles was solubilized by nonionic detergent C12E8 and purified in a reactive red-120 agrose affinity column.Determined by 7.5% SDS-PAGE,the purity of Ca2+-ATPase was increased from 65% to 99% and the purified Ca2+-ATPase exhibited higher ATP hydrolysis activity.
Keywords:sarcoplasmic reticulum Ca2+-ATPase  reactive red-120 agrose  affinity gel filtration
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