Watson D C, Peters E H, Dixon G H
Eur J Biochem. 1977 Mar 15;74(1):53-60. doi: 10.1111/j.1432-1033.1977.tb11365.x.
A specific non-histone chromatin-associated protein, having a high content of both acidic and basic amino acids has been isolated from the chromatin of rainbow trout (Salmo gairdnerii) testis cells. The protein has been prepared by the extraction of chromatin with 0.35 M sodium chloride and purified by chromatography on carboxymethyl-cellulose with a gradient of lithium chloride at pH 9.0. The amino acid sequence of the first 29 residues of the amino-terminal region has been determined using an automatic protein sequencer. The primary structure of this protein differs from that of any of the histones yet sequenced and, therefore, cannot be a degradation produce of any of them. Moreover, the N-terminal amino acid sequence shows considerable similarity to the HMG-1 and HMG-2 chromosomal proteins described by Goodwin et al. [Eur. J. Biochem. 38, 14-19 (1973)] whose-N-terminal sequences were also determined in this laboratory.
从虹鳟(Salmo gairdnerii)睾丸细胞的染色质中分离出一种特定的非组蛋白染色质相关蛋白,该蛋白富含酸性和碱性氨基酸。该蛋白通过用0.35M氯化钠提取染色质制备,并在pH 9.0的条件下用氯化锂梯度在羧甲基纤维素上进行色谱纯化。使用自动蛋白质测序仪测定了氨基末端区域前29个残基的氨基酸序列。该蛋白的一级结构与任何已测序的组蛋白都不同,因此不可能是它们的降解产物。此外,其N端氨基酸序列与Goodwin等人[《欧洲生物化学杂志》38, 14 - 19 (1973)]描述的HMG - 1和HMG - 2染色体蛋白有相当大的相似性,其N端序列也是在本实验室测定的。