牛源丝切蛋白II的纯化与特性分析。肌动蛋白、聚（L-脯氨酸）及肌醇磷脂结合
Purification and characterization of bovine profilin II. Actin, poly(L-proline) and inositolphospholipid binding.
作者信息
Lambrechts A, van Damme J, Goethals M, Vandekerckhove J, Ampe C
机构信息
Flanders Institute of Biotechnology, University Ghent, Belgium.
出版信息
Eur J Biochem. 1995 May 15;230(1):281-6.
We purified profilin from bovine brain and were able to separate the two isoforms present in this tissue. Since functional characteristics for profilin II are lacking, we assayed the actin, the phosphatidylinositol 4,5-bisphosphate and the poly(L-proline) binding properties of this isoform. Profilin II binds actin with a similar affinity to that of profilin I, although it inhibits actin polymerization more strongly than profilin I under non-equilibrium conditions. Profilin II also binds the anionic phospholipid phosphatidylinositol 4,5-bisphosphate. Profilin II binds to poly(L-proline) more strongly than does profilin I; this is especially evident at more acidic pH values. This difference is explained by an amino acid exchange in the carboxy-terminal part of the protein which has been implicated in poly(L-proline) binding [Björkegren, C., Rozycki, M., Schutt, C., Lindberg, U. & Karlsson, R. (1993) FEBS Lett. 333, 123-126; Metzler, W., Bell, A., Ernst, E., Lavoie, T. & Mueller, L. (1994) J. Biol. Chem. 369, 4620-4625].
我们从牛脑中纯化了肌动蛋白结合蛋白，并成功分离出该组织中存在的两种同工型。由于缺乏对肌动蛋白结合蛋白II功能特性的研究，我们检测了该同工型与肌动蛋白、磷脂酰肌醇4,5-二磷酸以及聚（L-脯氨酸）的结合特性。肌动蛋白结合蛋白II与肌动蛋白的结合亲和力与肌动蛋白结合蛋白I相似，不过在非平衡条件下，它比肌动蛋白结合蛋白I更强烈地抑制肌动蛋白聚合。肌动蛋白结合蛋白II还能结合阴离子磷脂磷脂酰肌醇4,5-二磷酸。肌动蛋白结合蛋白II与聚（L-脯氨酸）的结合比肌动蛋白结合蛋白I更紧密；在更酸性的pH值条件下，这种差异尤为明显。这种差异可由该蛋白羧基末端的一个氨基酸交换来解释，这一交换与聚（L-脯氨酸）的结合有关[比约克格伦，C.，罗齐茨基，M.，舒特，C.，林德伯格，U. & 卡尔松，R.（1993年）《欧洲生物化学学会联合会快报》333，123 - 126；梅茨勒，W.，贝尔，A.，恩斯特，E.，拉沃伊，T. & 米勒，L.（1994年）《生物化学杂志》369，4620 - 4625]。
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