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pubmed-article:890567pubmed:abstractTextAmino acid composition and tryptic fingerprints of rye (Secal cereale) H1, H2B (PH1), and H2A(PHII) histones indicate the presence of major differences between these and the corresponding calf or rabbit fractions. In addition to variations for other amino acids, fraction H1 from rye contains twice as much arginine as the corresponding animal fraction; the plant H2B (PHI) and H2A (PHII) histones show lysine to arginine ratios greater than those of their animal counterparts. The tryptic maps of the same proteins appear to differ between plants and animals by the number and the general pattern of the peptides, as well as by the quantity and distribution of the arginine-containing peptides. Such results suggest the presence of differences in the primary structure of the calf and rye lysine-rich and moderately lysine-rich histones. Furthermore, the possibility is ruled out that each of these plant histones consists of an animal-like protein with an additional segment of 20--30 amino acid residues. On the other hand, the rye and calf arginine-rich fractions H3 and H4 show similar amino acid compositions and tryptic peptides maps.lld:pubmed
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pubmed-article:890567pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:890567pubmed:year1977lld:pubmed
pubmed-article:890567pubmed:articleTitleComparative study of rye and thymus histones: amino acid analysis and tryptic fingerprinting.lld:pubmed
pubmed-article:890567pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:890567pubmed:publicationTypeComparative Studylld:pubmed