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Release of ribonucleoprotein during digestion of rat testis chromatin with deoxyribonuclease II (3.1.4.6).

作者信息

Grimes S R

出版信息

Comp Biochem Physiol B. 1984;78(3):633-41. doi: 10.1016/0305-0491(84)90110-x.

DOI:10.1016/0305-0491(84)90110-x
PMID:6478794
Abstract

The composition of rat testis chromatin proteins in fractions produced by limited DNase II digestion followed by differential precipitation with MgCl2 has been studied. Over 50% of the acid-soluble proteins in the soluble chromatin fraction appeared to be quite similar to proteins which are associated with ribonucleoprotein (RNP) particles in HeLa cells. Although the ratios of the testis RNP protein components differed from those of HeLa RNP particles, the three major polypeptides were most similar to the HeLa components designated A2, B2, and C1. The soluble chromatin fraction was also enriched in the high mobility group proteins HMG1 and HMG2.

摘要

相似文献

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