胸腺肌动蛋白：制备与特性

Thymus actin: preparation and characterization.

作者信息

Ajtai K, Dankó S, Harsányi V, Bíró E N

出版信息

Acta Biochim Biophys Acad Sci Hung. 1979;14(1-2):43-52.

Abstract

A combination of the C-gamma alumina adsorption technique of Lindberg, U. Skoog, L. 1970. Eur. J. Biochem. 13 326-335 with the traditional actin purification procedure (polymerization-depolymerization) yielded a simple method for the preparation of actin from fresh or acetone-dried thymus tissue. Actin obtained by this procedure from thymus was homogeneous and comigrated with skeletal actin in SDS gel electrophoresis. In isoelectric focusing it was shown to contain beta and gamma actin. Thymus actin polymerized poorly or not at all. It was native, however, as judged from its DN-ase I inhibiting activity which equalled that of skeletal actin. It also activated skeletal myosin ATP-ase but to a lesser extent than skeletal actin. On addition of HMM to thymus G actin, decorated filaments formed abundantly.

摘要

将林德伯格、U. 斯科格、L. 1970年在《欧洲生物化学杂志》第13卷第326 - 335页中描述的C - γ氧化铝吸附技术与传统的肌动蛋白纯化程序（聚合 - 解聚）相结合，得到了一种从新鲜或丙酮干燥的胸腺组织中制备肌动蛋白的简单方法。通过该程序从胸腺获得的肌动蛋白是均质的，并且在SDS凝胶电泳中与骨骼肌肌动蛋白共迁移。在等电聚焦中显示其含有β和γ肌动蛋白。胸腺肌动蛋白聚合不良或根本不聚合。然而，从其DN - 酶I抑制活性判断，它是天然的，该活性与骨骼肌肌动蛋白相当。它也能激活骨骼肌肌球蛋白ATP酶，但程度低于骨骼肌肌动蛋白。向胸腺G肌动蛋白中添加重酶解肌球蛋白后，大量形成了装饰丝。