Dumuis-Kervabon A, Parello J
C R Acad Sci III. 1984;299(7):185-8.
The proteolysis of the chromatin core particle by the arginine-specific endopeptidase clostripain yields a new nucleoprotein particle containing an unaltered DNA fragment of about 145 base pairs in length and a protein octameric core made up of twice the four histone fragments H2A, H2B, H3 and H4. This composition is suggested by the molecular weight of about 180 kd determined for the new particle by small angle neutron scattering. The histone fragments differ by about 2-3 kd each from the initial histones H2A, H2B, H3 and H4 and they correspond to the cleavage of the N-terminal part of the sequence (20-30 residues). A preliminary investigation by thermal denaturation, circular dichroism and small angle neutron scattering (measurement of a radius of gyration by the H2O-D2O contrast variation technique) indicates that the spatial organization of the new chromatin particle closely resembles that of the initial core particle.
精氨酸特异性内肽酶梭菌蛋白酶对染色质核心颗粒进行蛋白水解，产生一种新的核蛋白颗粒，该颗粒包含一个长度约为145个碱基对的未改变的DNA片段和一个由两倍数量的四种组蛋白片段H2A、H2B、H3和H4组成的蛋白质八聚体核心。小角中子散射测定新颗粒的分子量约为180kd，由此推测出这种组成。每个组蛋白片段与初始组蛋白H2A、H2B、H3和H4相比，分子量相差约2 - 3kd，它们对应于序列N端部分（20 - 30个残基）的切割。通过热变性、圆二色性和小角中子散射（采用H2O - D2O对比变化技术测量回转半径）进行的初步研究表明，新染色质颗粒的空间组织与初始核心颗粒非常相似。
