Comparative enzymatic degradation of H1 subfractions from Syrian hamster tissues.
نویسندگان
چکیده
An additional hydrolysis site recognized by thrombin on histone H1 molecules was found. Snakes venom proteases from Agkistrodon rhodostoma, Bothrops marajoensis and Bothrops moojeni were further used for the analysis of H1 histones. The presence of the main cleavage site on H1 histone molecules has been established. This site is localized on main N-terminal thrombin peptide. The main venom protease peptides obtained from different H1 subfractions preserve differences of electrophoretic mobility in acid-urea polyacrylamide gels typical for the initial H1 subfractions.
منابع مشابه
Distribution of the H1 histone subfractions in Syrian hamster chromatin fractions.
Chromatin from two Syrian hamster tissues: the Kirkman-Robbins hepatoma and the liver, has been separated into soluble (S) and insoluble (P) fractions. Both fractions contain the complete set of five main histones but differ in respect of H1 subfractions. The hepatoma chromatin is known to contain an unusual H1 subfraction, H1 slow [12, 13], probably identical with a similar subfraction present...
متن کاملDistribution of the H I Histone Subfractions in Syrian Hamster Chromatin Fractions
Chromatin from two Syrian hamster tissues: the Kirkman-Robbins hepatoma and the liver, has been separated into soluble (S) and insoluble (P) fractions. Both fractions contain the complete set of five main histones but differ in respect of HI subfractions. The hepatoma chromatin is known to contain an unusual HI subfraction, HI slow [12, 13], probably identical with a similar subfration present ...
متن کاملA low-electrophoretic-mobility H1 histone subfraction from Kirkman-Robbins hamster hepatoma.
A protein showing lower electrophoretic mobility in acidic urea polyacrylamide gels than did the usual histone H1 subfractions has been detected among the H1 histones extracted from chromatin of a transplantable hamster hepatoma, originally induced by Kirkman and Robbins. It was proved to be a true H1 histone subfraction. It differs from the remaining ones by the total chain length, amino acid ...
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ورودعنوان ژورنال:
- Zeitschrift fur Naturforschung. C, Journal of biosciences
دوره 41 7-8 شماره
صفحات -
تاریخ انتشار 1986