Kravchenko L S, Oksman A Ia, Tereshin I M
Biokhimiia. 1977 Apr;42(4):687-92.
A relationship between the previously observed degradation of dog kidney chromatin histones induced by polyene antibiotics, and a change in enzymatic activity of neutral histone protease or proteases localized on the outer nuclear membrane was studied. It was shown that in the course of proteolysis of chromatin isolated from the nuclei after treatment by Triton X-100 nistatin inhibits neutral histone proteases as can be evidenced from the amount of the amino groups formed and the data of electrophoretic analysis of chromatin histones. The inhibitory effect of nistatin is sharply enhanced with an increase in its concentration. It is found that in the course of proteolysis of chromatin isolated from the nuclei untreated with Triton X-100, nistatin increases the degree of acid-soluble protein degradation. The latter effect is probably due to the stimulation of the enzymatic activity of proteases localized on the outer nuclear membrane by nistatin.
研究了先前观察到的多烯抗生素诱导犬肾染色质组蛋白降解与位于外核膜上的中性组蛋白蛋白酶或蛋白酶的酶活性变化之间的关系。结果表明，在用Triton X - 100处理后从细胞核中分离出的染色质进行蛋白水解过程中，制霉菌素抑制中性组蛋白蛋白酶，这可以从形成的氨基数量和染色质组蛋白的电泳分析数据得到证明。制霉菌素的抑制作用随着其浓度的增加而急剧增强。发现在用Triton X - 100未处理的细胞核中分离出的染色质进行蛋白水解过程中，制霉菌素增加了酸溶性蛋白的降解程度。后一种效应可能是由于制霉菌素刺激了位于外核膜上的蛋白酶的酶活性。
