Abstract
The reactivities of the two cysteine thiol groups of calf thymus F3 histone were investigated using 5,5′-dithiobis-[2- nitrobenzoic acid], (DTNB). In isolated histone, both thiol groups were available for reaction. However, analysis of reaction profiles of native deoxyribonucleohistone, (DNH), in various solvent conditions, together with gel electrophoresis studies of DNH modified with DTNB, showed that only one of the thiol groups is normally modified by the reagent. If NaCl is present (above 1.OM) the other thiol group can also be modified. The reactivities of both groups were largely independent of the degree of DNH supercoiling and of the binding of F3 to the DNA.
Full text
PDF












Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- ALLFREY V. G., MIRSKY A. E. Evidence for the complete DNA-dependence of RNA synthesis in isolated thymus nuclei. Proc Natl Acad Sci U S A. 1962 Sep 15;48:1590–1596. doi: 10.1073/pnas.48.9.1590. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brandt W. F., Von Holt C. The complete amino acid sequence of histone F(3) from chicken erythrocytes. FEBS Lett. 1972 Jul 1;23(3):357–360. doi: 10.1016/0014-5793(72)80315-6. [DOI] [PubMed] [Google Scholar]
- Chatterjee S., Walker I. O. The modification of deoxyribonucleohistone by trypsin and chymotrypsin. Eur J Biochem. 1973 May 2;34(3):519–526. doi: 10.1111/j.1432-1033.1973.tb02789.x. [DOI] [PubMed] [Google Scholar]
- DeLange R. J., Fambrough D. M., Smith E. L., Bonner J. Calf and pea histone IV. 3. Complete amino acid sequence of pea seedling histone IV; comparison with the homologous calf thymus histone. J Biol Chem. 1969 Oct 25;244(20):5669–5679. [PubMed] [Google Scholar]
- DeLange R. J., Hooper J. A., Smith E. L. Histone 3. 3. Sequence studies on the cyanogen bromide peptides; complete amino acid sequence of calf thymus histone 3. J Biol Chem. 1973 May 10;248(9):3261–3274. [PubMed] [Google Scholar]
- ELLMAN G. L. Tissue sulfhydryl groups. Arch Biochem Biophys. 1959 May;82(1):70–77. doi: 10.1016/0003-9861(59)90090-6. [DOI] [PubMed] [Google Scholar]
- Ewars P. A., Sooter K. V. Ultracentrifuge tudies of histone fractions from calf thymus deoxyribonucleoprotein. Biochem J. 1969 Sep;114(2):227–235. doi: 10.1042/bj1140227. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HUANG R. C., BONNER J. Histone, a suppressor of chromosomal RNA synthesis. Proc Natl Acad Sci U S A. 1962 Jul 15;48:1216–1222. doi: 10.1073/pnas.48.7.1216. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Henson P., Walker I. O. The partial dissociation of nucleohistone by salts. Circular dichroism and denaturation studies. Eur J Biochem. 1970 Nov;16(3):524–531. doi: 10.1111/j.1432-1033.1970.tb01112.x. [DOI] [PubMed] [Google Scholar]
- Henson P., Walker I. O. The structure of nucleohistone. Hydrodynamic behaviour at high ionic strength. Eur J Biochem. 1971 Sep 13;22(1):1–4. doi: 10.1111/j.1432-1033.1971.tb01506.x. [DOI] [PubMed] [Google Scholar]
- Hooper J. A., Smith E. L., Sommer K. R., Chalkley R. Histone 3. IV. Amino acid sequence of histone 3 of the testes of the carp, Letiobus bubalus. J Biol Chem. 1973 May 10;248(9):3275–3279. [PubMed] [Google Scholar]
- Huberman J. A., Attardi G. Isolation of metaphase chromosomes from HeLa cells. J Cell Biol. 1966 Oct;31(1):95–105. doi: 10.1083/jcb.31.1.95. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LEE M. F., WALKER I. O., PEACOCKE A. R. Thymus deoxyribonucleoprotein. IV. Thermal denaturation. Biochim Biophys Acta. 1963 Jun 25;72:310–316. doi: 10.1016/0006-3002(63)90246-4. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Marzluff W. F., Jr, Sanders L. A., Miller D. M., McCarty K. S. Two chemically and metabolically distinct forms of calf thymus histone F3. J Biol Chem. 1972 Apr 10;247(7):2026–2033. [PubMed] [Google Scholar]
- Palau J., Padrós E. Crevices containing cysteine in the tertiary structure of calf thymus histone F3. FEBS Lett. 1972 Oct 15;27(1):157–160. doi: 10.1016/0014-5793(72)80431-9. [DOI] [PubMed] [Google Scholar]
- Panyim S., Chalkley R. High resolution acrylamide gel electrophoresis of histones. Arch Biochem Biophys. 1969 Mar;130(1):337–346. doi: 10.1016/0003-9861(69)90042-3. [DOI] [PubMed] [Google Scholar]
- Panyim S., Chalkley R. The heterogeneity of histones. I. A quantitative analysis of calf histones in very long polyacrylamide gels. Biochemistry. 1969 Oct;8(10):3972–3979. doi: 10.1021/bi00838a013. [DOI] [PubMed] [Google Scholar]
- Panyim S., Sommer K. R., Chalkley R. Oxidation of the cysteine-containing histone F3. Detection of an evolutionary mutation in a conservative histone. Biochemistry. 1971 Oct 12;10(21):3911–3917. doi: 10.1021/bi00797a018. [DOI] [PubMed] [Google Scholar]
- Pardon J. F., Wilkins M. H., Richards B. M. Super-helical model for nucleohistone. Nature. 1967 Jul 29;215(5100):508–509. doi: 10.1038/215508a0. [DOI] [PubMed] [Google Scholar]
- Patthy L., Smith E. L. Histone 3. V. The amino acid sequence of pea embryo histone 3. J Biol Chem. 1973 Oct 10;248(19):6834–6840. [PubMed] [Google Scholar]
- Prothero J. W. Correlation between the distribution of amino acids and alpha helices. Biophys J. 1966 May;6(3):367–370. doi: 10.1016/S0006-3495(66)86662-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Robyt J. F., Ackerman R. J., Chittenden C. G. Reaction of protein disulfide groups with Ellman's reagent: a case study of the number of sulfhydryl and disulfide groups in Aspergillus oryzae -amylase, papain, and lysozyme. Arch Biochem Biophys. 1971 Nov;147(1):262–269. doi: 10.1016/0003-9861(71)90334-1. [DOI] [PubMed] [Google Scholar]
- Sadgopal A., Bonner J. Proteins of interphase and metaphase chromosomes compared. Biochim Biophys Acta. 1970 Apr 28;207(1):227–239. doi: 10.1016/0005-2795(70)90154-6. [DOI] [PubMed] [Google Scholar]
- Schiffer M., Edmundson A. B. Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. Biophys J. 1967 Mar;7(2):121–135. doi: 10.1016/S0006-3495(67)86579-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Skidmore C., Walker I. O., Pardon J. F., Richards B. M. The structure of partially histone depleted nucleohistone. FEBS Lett. 1973 May 15;32(1):175–178. doi: 10.1016/0014-5793(73)80765-3. [DOI] [PubMed] [Google Scholar]
- Walker I. O. Electrometric and spectrophotometric titration of histone and deoxyribonucleohistone. J Mol Biol. 1965 Dec;14(2):381–398. doi: 10.1016/s0022-2836(65)80189-9. [DOI] [PubMed] [Google Scholar]
