A PROTEASE ACTIVITY IS ASSOCIATED WITH TESTICULAR CHROMATIN OF THE MOUSE
A PROTEASE ACTIVITY IS ASSOCIATED WITH TESTICULAR CHROMATIN OF THE MOUSE
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DOI：
10.1095/biolreprod36.2.471
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发表时间：
1987-03-01
影响因子：
3.6
通讯作者：
BHATNAGAR, YM
中科院分区：
文献类型：
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作者：
FAULKNER, RD;BHATNAGAR, YM
与微球菌核酸酶溶解小鼠精管染色质相关的蛋白酶活性已被表征。3 M尿素刺激组蛋白H1和核心组蛋白的蛋白水解。该蛋白酶的最适pH值在pH 8 ~ 9之间，活性不受胰蛋白酶或凝乳胰蛋白酶活性位点抑制剂的抑制。Leupeptin是一种有效的低浓度蛋白酶抑制剂。新生儿和青春期前小鼠的可溶性染色质直到出生后三到四周才缺乏这种蛋白水解活性。蛋白酶活性局限于二核小体和更高的低聚体，但在单核小体群体中缺乏，这表明它与连接体DNA有关。大鼠睾丸可溶性染色质显然缺乏这种蛋白酶活性。该蛋白酶的发育表达及其原位定位与小鼠精子发生过程中组蛋白位移的作用一致。
A protease activity associated with the micrococcal nuclease-solubilized chromatin from mouse seminiferous tubules has been characterized. Proteolysis of histone H1 and core histones is stimulated in the presence of 3 M urea. The pH optimum of this protease is between pH 8 and 9, and the activity is not inhibited by trypsin or chymotrypsin-active site inhibitors. Leupeptin is an effective inhibitor of the protease at low concentrations. Soluble chromatin from neonatal and prepubertal mice lacks this proteolytic activity until three to four weeks after birth. That the protease activity is localized in the dinucleosomes and higher oligomers but is lacking in mononucleosome populations suggests its association with the linker DNA. Rat testis-soluble chromatin apparently lacks such a protease activity. The developmental expression of this protease and its in situ localization are consistent with a role in histone displacement during mouse spermiogenesis.