H1(0) histones of normal and cancer human cells. Amino acid composition of H1 purified by polyacrylamide gel electrophoresis.

Abstract

H1 histones were purified by preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis from human lung carcinoma (line DMS79), human hepatoblastoma (HepG2), human adult lung and human adult and fetal liver. The purified human H1 histones were analyzed for their amino acid composition and terminal residues. The comparative analysis of the amino acid compositions of the different human H1 histones showed that: all the H1 preparations have the characteristically high lysine content associated with a low arginine content, which distinguishes outer histones from core histones; H1 is distinguishable from other H1 histones by the presence of methionine and histidine; H1 histones from human adult, fetal and cancer cells are very similar in amino acid composition, and in cancer cells the level of the H1 histone is not inversely related with cell growth rate nor with the expression of the alpha-fetoprotein gene.

• Authors: F Gabrielli, A Tsugita
• Journal: Molecular and cellular biochemistry (Mol Cell Biochem) Vol. 71 Issue 2 Pg. 129-34 (Aug 1986) ISSN: 0300-8177 [Print] Netherlands
• PMID: 3022119 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amino Acids
• Histones
• Arginine
• Lysine

Topics

• Amino Acids (analysis)
• Arginine (analysis)
• Carcinoma, Hepatocellular (chemistry)
• Cell Line
• Histones (analysis)
• Humans
• Liver (chemistry, embryology)
• Liver Neoplasms (chemistry)
• Lung (chemistry)
• Lung Neoplasms (chemistry)
• Lysine (analysis)
• Neoplasms (chemistry)