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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/8822
Title: Oxidation of the Cysteine-Containing Histone F3. Detection of an Evolutionary Mutation in a Conservative Histone
Authors: Sakol Panyim
K. R. Sommer
Roger Chalkley
University of Iowa
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Oct-1971
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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0015221164&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/8822
ISSN: 15204995
00062960
Appears in Collections:Scopus 1969-1990

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