Publication: Oxidation of the Cysteine-Containing Histone F3. Detection of an Evolutionary Mutation in a Conservative Histone
Issued Date
1971-10-01
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ISSN
15204995
00062960
00062960
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2-s2.0-0015221164
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Mahidol University
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SCOPUS
Bibliographic Citation
Biochemistry. Vol.10, No.21 (1971), 3911-3917
Suggested Citation
Sakol Panyim, K. R. Sommer, Roger Chalkley Oxidation of the Cysteine-Containing Histone F3. Detection of an Evolutionary Mutation in a Conservative Histone. Biochemistry. Vol.10, No.21 (1971), 3911-3917. doi:10.1021/bi00797a018 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/8822
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Title
Oxidation of the Cysteine-Containing Histone F3. Detection of an Evolutionary Mutation in a Conservative Histone
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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.