来自稳态胸腺激素（HTHα和HTHβ）制剂的两条多肽链的一级结构与两种组蛋白完全相同。
The primary structure of two polypeptide chains from preparations of homeostatic thymus hormone (HTH alpha and HTH beta) entire-chain identities to two histones.
作者信息
Reichhart R, Jörnvall H, Carlquist M, Zeppezauer M
出版信息
FEBS Lett. 1985 Aug 19;188(1):63-7. doi: 10.1016/0014-5793(85)80875-9.
PMID:3894052
Abstract
The primary structures of the 2 polypeptide chains (HTH alpha and HTH beta) of the homeostatic thymus hormone (HTH) were determined. The entire structures were found to be identical to those of histones H2A and H2B, respectively, without evidence for sub-types, proteolytic processings, or other peptide fragments. The results show that suggestions for new extranuclear and hormone-like histone functions apply to HTH preparations with intact protein chains of the H2 histones.
摘要
确定了稳态胸腺激素（HTH）的两条多肽链（HTHα和HTHβ）的一级结构。发现其完整结构分别与组蛋白H2A和H2B的结构相同，未发现亚型、蛋白水解加工或其他肽片段的证据。结果表明，关于新的核外和类激素组蛋白功能的推测适用于具有完整H2组蛋白蛋白链的HTH制剂。
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