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- W2392899869 abstract "The acid-soluble proteins of Oxyr-rhis marina nuclei contain two electro-phoric bands in the histone district onpolyacrylamide in comparison with thehistones from calf thymus nuclei.Theelectrophoric mobility of one of themis similar to histone H4 and the otherone is similar to histone H1.Theelectrophorisis on high-resolution poly-acrylamide gradient slab gel shows thatthe H4-like protein consists of threesub-bands and the electrophoresis withtwo dimensional acidic urea-SDS gelindicates that it's molecular weight isabout 16,000.The results of amino-acid analysis indicate that the H4-likeprotein is a lysine-rich basic protein;thebasic amino acid residues amount to25% of the total amino acid residues;the ratio of basic and acidic amino acidsis 1.5 and lysine:arginine is 9:1." @default.
- W2392899869 created "2016-06-24" @default.
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- W2392899869 date "1983-01-01" @default.
- W2392899869 modified "2023-09-26" @default.
- W2392899869 title "THE PRELIMINARY STUDIES ON THE CHROMATIN STRUCTURE OF DINOFLAGELLATE,OXYRRHIS MARINA:ACID-SOLUBLE PROTEINS" @default.
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