Open AccessThe Purification, Characterization and Partial Sequence Determination of a Trout Testis Non‐histone Protein, HMG‐T
Author(s) -
WATSON David C.,
PETERS Erwin H.,
DIXON Gordon H.
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11365.x
Subject(s) - chromatin , histone , biology , biochemistry , peptide sequence , acetylation , microbiology and biotechnology , amino acid , salmo , rainbow trout , dna , gene , fishery , fish <actinopterygii>
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 gairdneril ) 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 product 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.