Chromatin proteins associated with micrococcal nuclease-sensitive and nuclease-resistant chromatin fractions of Kirkman-Robbins hepatoma and hamster liver

• Published in: Molecular biology reports 1984-07, Vol.10 (1), p.31-39
• Main Authors: LIPINSKA, A, KILIANSKA, Z, KRAJEWSKA, W. M, KŁYSZEJKO-STEFANOWICZ, L
• Format: Article
• Language: English
• Subjects: Animals; Biological and medical sciences; Chromatin - metabolism; Chromatin. Chromosome; Chromosomal Proteins, Non-Histone - metabolism; Cricetinae; Densitometry; Fundamental and applied biological sciences. Psychology; Histones - metabolism; Liver - analysis; Liver Neoplasms, Experimental - analysis; Micrococcal Nuclease - metabolism; Molecular and cellular biology; Molecular genetics; Molecular Weight; Peptide Hydrolases - metabolism
• ISSN: 0301-4851; 1573-4978
• DOI: 10.1007/BF00775151

Micrococcal nuclease-sensitive (SP) and nuclease-resistant (PP) chromatin fractions from Kirkman-Robbins hepatoma and hamster liver were obtained. The molecular distribution of three non-histone proteins (NHCP1, NHCP2 and NHCP3), histones, and chromatin-bound protease activity between SP and PP fractions of both tissues was compared. Differences, mainly of quantitative nature, among non-histone proteins of neoplastic and normal tissue were observed. Moreover, it was found that polypeptides with mol. wt 81 000 (NHCP1), 39 000 (NHCP2) and 21 000, 35 000, 37 000 (NHCP1), 70 000, 112 000, 141 000, 157 000 (NHCP2), 30 000-33 000 (NHCP3) were associated only with the nuclease-sensitive part of chromatin of hepatoma and normal tissue, respectively. A major difference in histone composition of hamster hepatoma and liver concerns histones H2A and H1. Furthermore, an enrichment of high mobility group proteins as well as other soluble non-histone proteins in an acid extract of the SP fraction was observed. Apparently chromatin-bound protease activity can be found in both fractions of chromatin.