Sakol PanyimK. R. SommerRoger ChalkleyUniversity of IowaMahidol University2018-02-272018-02-271971-10-01Biochemistry. Vol.10, No.21 (1971), 3911-391715204995000629602-s2.0-0015221164https://repository.li.mahidol.ac.th/handle/20.500.14594/8822All 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.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1021/bi00797a018