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|Title:||Oxidation of the Cysteine-Containing Histone F3. Detection of an Evolutionary Mutation in a Conservative Histone|
K. R. Sommer
University of Iowa
|Keywords:||Biochemistry, Genetics and Molecular Biology|
|Citation:||Biochemistry. Vol.10, No.21 (1971), 3911-3917|
|Abstract:||All creatures we have examined, including plants, invertebrates, and vertebrates up to and including rodents, contain a single cysteine residue in their F3 histone. Mammals moee highly evolved than rodents contain two such cysteine residues. The presence of the additional cysteine affords a moee complex oxidation pattern and this has been documented. Thus, in contrast to those F3 molecules which contain a single cysteine residue and have a single dimer oxidation product, the F3 molecules with two cysteine residues can form an intramolecular disulfide bond (in solutions of high dielectric constant or at pH 8.0), a series of dimers with one or two disulfide bonds (in aqueous acetic acid), or a series of higher polymers (at high monomer concentrations). There is no evidence for histone disulfide-bond formation in interphase nuclei. © 1971, American Chemical Society. All rights reserved.|
|Appears in Collections:||Scopus 1969-1990|
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