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. 1975 Feb 1;64(2):389–397. doi: 10.1083/jcb.64.2.389

Electrophoretic analysis of liver and testis histones of the frog Rana pipiens

PMCID: PMC2109491  PMID: 1078823

Abstract

Histones were extracted from frog livers and testes and analyzed by electrophoresis on long polyacrylamide gels and on sodium dodecyl sulfate (SDS)-containing polyacrylamide gels. Frog histones were found to be similar to those of calf thymus except that frog histone fraction F2A2 showed a marked dependence on the temperature at which the long gels were run, and frog histone fraction F3 could be separated from frog F2B on SDS-containing gels. Comparisons between frog liver and frog testis histones indicated that the testis contains as its major F1 component a fast migrating species not found in liver. Testis histones also showed less microheterogeneity of fractions F3 and F2A1 than liver histones. These were the only differences observed between liver and testis histones, even when testis histones were prepared from sperm suspensions that were rich in cells in the late stages of spermiogenesis. Thus it seems that, in Rana, the electrophoretic properties of the basic proteins of sperm differ from those of somatic cells only in the nature of histone F1 and in the degree of microheterogeneity of fractions F2A1 and F3.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bartley J., Chalkley R. Further studies of a thymus nucleohistone-associated protease. J Biol Chem. 1970 Sep 10;245(17):4286–4292. [PubMed] [Google Scholar]
  2. Bloch D. P. A catalog of sperm histones. Genetics. 1969;61(1 Suppl):93–111. [PubMed] [Google Scholar]
  3. Brandt W. F., Strickland W. N., Morgan M., Von Holt C. Comparison of the n-terminal amino acid sequences of histone F3 from a mammal, a bird, a shark, an echinoderm, a mollusc and a plant. FEBS Lett. 1974 Mar 15;40(1):167–172. doi: 10.1016/0014-5793(74)80919-1. [DOI] [PubMed] [Google Scholar]
  4. Bustin M., Cole R. D. Species and organ specificity in very lysine-rich histones. J Biol Chem. 1968 Sep 10;243(17):4500–4505. [PubMed] [Google Scholar]
  5. Bustin M., Stollar B. D. Immunochemical specificity in lysine-rich histone subfractions. J Biol Chem. 1972 Sep 25;247(18):5716–5721. [PubMed] [Google Scholar]
  6. DeLange R. J., Fambrough D. M., Smith E. L., Bonner J. Calf and pea histone IV. II. The complete amino acid sequence of calf thymus histone IV; presence of epsilon-N-acetyllysine. J Biol Chem. 1969 Jan 25;244(2):319–334. [PubMed] [Google Scholar]
  7. 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]
  8. Easton D., Chalkley R. High-resolution electrophoretic analysis of the histones from embryos and sperm of Arbacia punctulata. Exp Cell Res. 1972 Jun;72(2):502–508. doi: 10.1016/0014-4827(72)90020-1. [DOI] [PubMed] [Google Scholar]
  9. Gorovsky M. A., Carlson K., Rosenbaum J. L. Simple method for quantitive densitometry of polyacrylamide gels using fast green. Anal Biochem. 1970 Jun;35(2):359–370. doi: 10.1016/0003-2697(70)90196-x. [DOI] [PubMed] [Google Scholar]
  10. Gorovsky M. A., Pleger G. L., Keevert J. B., Johmann C. A. Studies on histone fraction F2A1 in macro- and micronuclei of Tetrahymena pyriformis. J Cell Biol. 1973 Jun;57(3):773–781. doi: 10.1083/jcb.57.3.773. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hayashi K., Matsutera E., Oba Y. A theoretical consideration of the abnormal behavior of histones on sodium dodecylsulfate gel electrophoresis. Biochim Biophys Acta. 1974 Mar 14;342(1):185–194. doi: 10.1016/0005-2795(74)90120-2. [DOI] [PubMed] [Google Scholar]
  12. Johmann C., Eckhardt R. A., Gorovsky M. A. The histones associated with condensed and extended chromatin of mouse liver. J Cell Biol. 1973 Jul;58(1):119–125. doi: 10.1083/jcb.58.1.119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kinkade J. M., Jr Qualitative species differences and quantitative tissue differences in the distribution of lysine-rich histones. J Biol Chem. 1969 Jun 25;244(12):3375–3386. [PubMed] [Google Scholar]
  14. Louie A. J., Dixon G. H. Kinetics of phosphorylation and dephosphorylation of testis histones and their possible role in determining chromosomal structure. Nat New Biol. 1973 Jun 6;243(127):164–168. doi: 10.1038/newbio243164a0. [DOI] [PubMed] [Google Scholar]
  15. Oliver D., Sommer K. R., Panyim S., Spiker S., Chalkley R. A modified procedure for fractionating histones. Biochem J. 1972 Sep;129(2):349–353. doi: 10.1042/bj1290349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Panyim S., Chalkley R. A new histone found only in mammalian tissues with little cell division. Biochem Biophys Res Commun. 1969 Dec 4;37(6):1042–1049. doi: 10.1016/0006-291x(69)90237-x. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. Panyim S., Chalkley R., Spiker S., Oliver D. Constant electrophoretic mobility of the cysteine-containing histone in plants and animals. Biochim Biophys Acta. 1970 Jul 27;214(1):216–221. doi: 10.1016/0005-2795(70)90086-3. [DOI] [PubMed] [Google Scholar]
  19. Panyim S., Chalkley R. The molecular weights of vertebrate histones exploiting a modified sodium dodecyl sulfate electrophoretic method. J Biol Chem. 1971 Dec 25;246(24):7557–7560. [PubMed] [Google Scholar]
  20. Sheridan W. F., Stern H. Histones of meiosis. Exp Cell Res. 1967 Feb;45(2):323–335. doi: 10.1016/0014-4827(67)90183-8. [DOI] [PubMed] [Google Scholar]
  21. Sherod D., Johnson G., Chalkley R. Phosphorylation of mouse ascites tumor cell lysine-rich histone. Biochemistry. 1970 Nov 10;9(23):4611–4615. doi: 10.1021/bi00825a022. [DOI] [PubMed] [Google Scholar]
  22. Zirkin B. R. The fine structure of nuclei during spermiogenesis in the leopard frog, Rana pipiens. J Ultrastruct Res. 1971 Jan;34(1):159–174. doi: 10.1016/s0022-5320(71)90011-6. [DOI] [PubMed] [Google Scholar]
  23. Zirkin B. R. The protein composition of nuclei during spermiogenesis in the leopard frog, Rana pipiens. Chromosoma. 1970;31(2):231–240. doi: 10.1007/BF00285150. [DOI] [PubMed] [Google Scholar]

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