Some Researches on Histones

نویسنده

  • J. A. V. Butler
چکیده

The histone extracted from calf thymus glands is a complex system of proteins, which can be fractionated by chromatography on carboxymethyl cellulose columns into three principal fractions (1) very lysine-rich, (2) moderately lysine-rich, (3) arginine-rich. When examined by starch gel chromatography each of these gives more than one band. Methods have been devised for further separation of the components in some cases. The components show characteristic differences in end groups and certain amino acids as well as in their basic character. Histones extracted from various rat tissues can be separated into similar fractions, of which the amino acid analyses are similar to those derived from calf thymus, within the experimental error. To this extent, no species or tissue specificity of the fractionated histones was observed. Although all the histone fractions contain approximately one basic amino acid to three non-basic amino acids their structure is not regular, as Phillips has shown that in certain fractions the number of non-basic groups between two basic groups may vary from 0 to seven or more. The possible functions of histones are discussed.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Sepsis and ARDS: The Dark Side of Histones

Despite advances in management over the last several decades, sepsis and acute respiratory distress syndrome (ARDS) still remain major clinical challenges and the leading causes of death for patients in intensive care units (ICUs) due to insufficient understanding of the pathophysiological mechanisms of these diseases. However, recent studies have shown that histones, also known as chromatin-ba...

متن کامل

COMPARATIVE STRUCTURAL STABILITY OF HISTONES BY INTERACTION OF SODIUM NDODECYL SULPHATE

The interaction of sodium n-dodecyl sulphate (SDS) with histones in phosphate buffer pH 6.4 has been studied spectroscopically and by equilibrium dialysis. The enthalpies of interaction and the spectroscopic data suggest different structural stability for histones-SDS interaction. The linear relation between enthaly and absorbtion was determined by the equation of m= , where m is the sta...

متن کامل

The effect of aspirin on the interaction of histone 05 and 05-DNA

The linker histones (H1 or H5) which play a key role in the folding of chromatin, are general repressors of gene expression. Nuclei of the mature chicken erythrocytes (and in some mammalian cells) contain both of them. Although the interaction of H5 with DNA is stronger than that of H1, it does not prevent the transcription of some erythroid-specific genes. It has been shown that some modificat...

متن کامل

Symmetrical modification within a nucleosome is not required globally for histone lysine methylation.

Two copies of each core histone exist in every nucleosome; however, it is not known whether both histones within a nucleosome are required to be symmetrically methylated at the same lysine residues. We report that for most lysine methylation states, wild-type histones paired with mutant, unmethylatable histones in mononucleosomes have comparable methylation levels to bulk histones. Our results ...

متن کامل

Histone Protein Glycation and Diabetes

Glycation and oxidation are two mechanisms that have been widely attributed with the generation of advanced glycation end products upon proteins in various pathological conditions. Histones being lysine and arginine rich are prone to these reactions and hence they are susceptible to glycoxidation reactions. Post translational modifications in the highly conserved basic core histone proteins are...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of General Physiology

دوره 45  شماره 

صفحات  -

تاریخ انتشار 1962