Partial resolution of the enzymes catalyzing photophosphorylation. XII. Purification and properties of an inhibitor isolated from chloroplast coupling factor 1.
Partial resolution of the enzymes catalyzing photophosphorylation. XII. Purification and properties of an inhibitor isolated from chloroplast coupling factor 1.
复制标题
催化光磷酸化的酶的部分分辨率。
DOI：
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发表时间：
1972
影响因子：
4.8
通讯作者：
E. Racker
中科院分区：
文献类型：
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作者：
N. Nelson;H. Nelson;E. Racker
摘要1.菠菜叶绿体偶联因子1在7M尿素溶液中能强烈抑制ATP酶活性。该抑制剂被鉴定为具有偶联因子的五个亚基中最小的亚基。2.该抑制剂被分离为纯蛋白质，估计分子量为13，000。氨基酸组成与线粒体ATP酶抑制剂不同。线粒体抑制剂仅抑制线粒体ATP酶，叶绿体抑制剂仅抑制叶绿体ATP酶。3.叶绿体抑制剂比线粒体抑制剂更难溶解，并且只能在尿素或去污剂存在的情况下才能保留在溶液中。与线粒体抑制剂一样，叶绿体抑制剂对热稳定，但对胰蛋白酶非常敏感。4.更大的疏水性和亲和力的叶绿体抑制剂的耦合因子有助于解释一些线粒体和叶绿体中的能量转导的生理差异，并负责以前的尝试，以隔离它的失败。
Abstract 1. Coupling factor 1 from spinach chloroplast dissolved in 7 m urea strongly inhibited the ATPase activity of the coupling factor. The inhibitor was identified with the smallest of the five subunits of the coupling factor. 2. The inhibitor was isolated as a pure protein and was estimated to have a molecular weight of 13,000. The amino acid composition was different from that of the inhibitor of mitochondrial ATPase. Mitochondrial inhibitor inhibited only mitochondrial ATPase; chloroplast inhibitor inhibited only chloroplast ATPase. 3. The chloroplast inhibitor is much more insoluble than the mitochondrial inhibitor and can be kept in solution only in the presence of urea or detergents. Like the mitochondrial inhibitor the chloroplast inhibitor is stable to heat but very sensitive to trypsin. 4. The greater hydrophobicity and affinity of the chloroplast inhibitor to the coupling factor helps to explain some of the physiological differences of energy transduction in mitochondria and chloroplasts and is responsible for the failure of previous attempts to isolate it.