Sánchez-Chiang L, Ponce O, Merino V
Biochem Int. 1984 Feb;8(2):237-44.
Chromatin from ammonia activated sea urchin eggs contains a proteolytic activity capable of hydrolyzing urea denatured casein at pH 8.0. The soluble fraction, obtained by treatment of chromatin with 0.7 M NaCl, presents a proteolytic activity which is about 16 times higher than that of the corresponding fraction from unfertilized eggs. Moreover, the SDS-PAGE profile of the soluble fraction from the ammonia activated eggs presents a greater number of bands and exhibits two groups of non histone proteins migrating near histone H1. The soluble proteolytic activity selectively digests certain non histone proteins of high and low molecular weight and histone H1 from the same fraction. Digestion products are formed. The effects of PMSF, sodium bisulfite and NaCl suggest the presence of more than one proteolytic activity in the soluble fraction from activated eggs. Our results sport the regulatory role of this enzyme activity based on the selective degradation of chromatin proteins.
来自氨激活海胆卵的染色质含有一种蛋白水解活性，能够在pH 8.0条件下水解尿素变性的酪蛋白。用0.7M NaCl处理染色质得到的可溶部分呈现出一种蛋白水解活性，该活性比未受精卵相应部分的活性高约16倍。此外，氨激活卵的可溶部分的SDS-PAGE图谱显示出更多的条带，并呈现出两组在组蛋白H1附近迁移的非组蛋白。可溶蛋白水解活性选择性地消化同一部分中某些高分子量和低分子量的非组蛋白以及组蛋白H1。形成了消化产物。苯甲基磺酰氟、亚硫酸氢钠和氯化钠的作用表明，激活卵的可溶部分存在不止一种蛋白水解活性。我们的结果支持了这种酶活性基于染色质蛋白选择性降解的调节作用。
