期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1980
卷号：77
期号：3
页码：1389-1393
DOI：10.1073/pnas.77.3.1389
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：A histone-like protein that is rich in alanine and lysine (protein AK) has been obtained in homogeneous form by high-resolution gel filtration of H2SO4 extracts of calf thymus chromatin. Protein AK: (i) migrates as a single band in polyacrylamide gel electrophoresis in both acetic acid/urea and sodium dodecyl sulfate; (ii) is a basic protein; (iii) lacks tryptophan; (iv) is not extracted from chromatin with 0.35 M NaCl; and (v) is not soluble in 0.75 M HClO4. Protein AK is distinguished from the high-mobility group (HMG) proteins on the basis of these latter solubility characteristics and from the histones and protein A24 on the basis of amino acid composition and distribution of tryptic peptides in two-dimensional chromato-electrophoresis. In addition, protein AK is distinguished from the HMG proteins, the histones, and protein A24 on the basis of its mobility in two polyacrylamide gel electrophoresis systems. The amino acid composition of protein AK resembles that of HU, a basic DNA-binding protein found in Escherichia coli.
