Characterization of calcium and phospholipid dependent protein kinase in isolated rat adipocytes.
Characterization of calcium and phospholipid dependent protein kinase in isolated rat adipocytes.
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分离的大鼠脂肪细胞中钙和磷脂依赖性蛋白激酶的表征。
DOI：
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发表时间：
1985
期刊：
影响因子：
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通讯作者：
M. Ingelman
中科院分区：
文献类型：
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作者：
G. Skoglund;A. Hansson;M. Ingelman
使用 DEAE-Sepharose CL-6B 部分纯化来自分离的大鼠脂肪细胞的钙和磷脂依赖性蛋白激酶（蛋白激酶 C）并进行表征。该酶被证明与从脑或脾中分离的激酶具有相似的特性。当使用组蛋白作为底物时，从 DEAE Sepharose CL-6B 级分中检测到等量的 cAMP 依赖性以及钙和磷脂依赖性激酶活性。蛋白激酶 C 的主要部分（72%）是从可溶性脂肪细胞部分中分离出来的。在膜部分中，质膜表现出最高的比活性。蛋白激酶制剂以高亲和力 (Kd = 2 nM) 结合 [3H]-佛波醇-12,13-二丁酸 (PDBU)，每个细胞的 PDBU 结合位点数量经计算为 63 000 个。
Calcium and phospholipid-dependent protein kinase (protein kinase C) from isolated rat adipocytes has been partially purified using DEAE-Sepharose CL-6B and characterized. The enzyme was shown to have similar properties as the kinase isolated from brain or spleen. When histone was used as substrate, an equal amount of cAMP-dependent and calcium and phospholipid-dependent kinase activity was detected from the DEAE Sepharose CL-6B fractions. The major part of protein kinase C (72%) was isolated from the soluble adipocyte fraction. Of the membranous fractions, the plasma membrane exhibited the highest specific activity. The protein kinase preparations bound [3H]-phorbol-12,13-dibutyrate (PDBU) with high affinity (Kd = 2 nM) and the number of PDBU binding sites per cell was calculated to 63 000.