Comparative enzymatic degradation of H1 subfractions from Syrian hamster tissues.
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.
D000818:Animals; D006224:Cricetinae; D004586:Electrophoresis; D006657:Histones / Q000032:analysis*; D006868:Hydrolysis; D008099:Liver / Q000378:metabolism; D008114:Liver Neoplasms, Experimental / Q000378:metabolism; D008647:Mesocricetus; D010447:Peptide Hydrolases / Q000378:metabolism; D012910:Snake Venoms / Q000032:analysis; D013347:Subcellular Fractions / Q000378:metabolism*; D013917:Thrombin / Q000378:metabolism
D006657:Histones; D012910:Snake Venoms; D010447:Peptide Hydrolases; D013917:Thrombin