一种来自牛小脑微粒部分的G蛋白偶联130 kDa磷脂酶C同工酶，即PLC-β4。
A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-beta 4, from the particulate fraction of bovine cerebellum.
作者信息
Min D S, Kim Y, Lee Y H, Suh P G, Ryu S H
机构信息
Department of Life Science, Pohang University of Science and Technology, South-Korea.
出版信息
FEBS Lett. 1993 Sep 27;331(1-2):38-42. doi: 10.1016/0014-5793(93)80293-4.
A 130 kDa PLC isozyme was purified from the particulate fraction of bovine cerebellum. This PLC was recognized by a polyclonal antiserum generated against the purified 97 kDa PLC-beta 4. Reconstitution of the purified 130 kDa PLC with the membranes of C6 Bu-1 cells in the presence of GTP gamma S or AlF4- resulted in PLC activation as well as the association of PLC with the membranes. Both the association and activation were revoked when the membrane was washed with 2 M KCl. The 97 kDa PLC-beta 4 did not associate with membranes. These data suggest that the 130 kDa PLC is the intact form of PLC-beta 4 the activity of which is likely to be regulated by a G-protein on the membrane.
从牛小脑的微粒部分纯化出一种130 kDa的磷脂酶C（PLC）同工酶。这种PLC可被针对纯化的97 kDa PLC-β4产生的多克隆抗血清识别。在存在GTPγS或AlF4-的情况下，将纯化的130 kDa PLC与C6 Bu-1细胞膜重建，导致PLC激活以及PLC与膜的结合。当用2 M KCl洗涤膜时，结合和激活都被消除。97 kDa PLC-β4不与膜结合。这些数据表明，130 kDa PLC是PLC-β4的完整形式，其活性可能受膜上G蛋白的调节。
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