MOUSE SPERM CHROMATIN PROTEINS - QUANTITATIVE ISOLATION AND PARTIAL CHARACTERIZATION
MOUSE SPERM CHROMATIN PROTEINS - QUANTITATIVE ISOLATION AND PARTIAL CHARACTERIZATION
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DOI：
10.1021/bi00637a021
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发表时间：
1977-01-01
期刊：
影响因子：
2.9
通讯作者：
WYROBEK, AJ
中科院分区：
文献类型：
--
作者：
BALHORN, R;GLEDHILL, BL;WYROBEK, AJ
描述了允许从小鼠附睾精子中定量提取染色质蛋白的条件。在用十六烷基三甲基溴化铵（CTAB）去除尾部后，分离这些蛋白质，使其不含污染的尾部蛋白质。如果没有这种处理，许多酸溶性尾蛋白与从部分纯化的头部分离的核蛋白共提取。以这种方式分离的蛋白质不需要预先用碘乙酰胺修饰，并且没有显示蛋白水解降解的证据。在酸性尿素聚丙烯酰胺凝胶中，99%的精子蛋白迁移为1条电泳带。证据表明，这一单一的带含有2鱼精蛋白样蛋白。
Conditions are described that permit the quantitative extraction of chromatin proteins from the epididymal sperm of the mouse. These proteins were isolated free of contaminating tail proteins following removal of the tails with cetyltrimethylammonium bromide (CTAB). Without this treatment, numerous acid-soluble tail proteins coextract with the nuclear proteins isolated from partially purified heads. The proteins isolated in this manner do not require prior modification with iodoacetamide and show no evidence of proteolytic degradation. In acid-urea polyacrylamide gels, 99% of the sperm protein migrates as 1 electrophoretic band. Evidence is presented that suggests that this single band contains 2 protamine-like proteins.