Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1970 Apr;117(3):509–512. doi: 10.1042/bj1170509

Histone F1 from rat thymus. Subfractionation and incorporation of [32P]phosphate in vitro

R H Buckingham 1, L A Stocken 1
PMCID: PMC1178954  PMID: 5419746

Abstract

Four subfractions of histone F1 from rat thymus were obtained by preparative polyacrylamide-gel electrophoresis. These subfractions are closely related in primary structure but show marked differences in radioactivity when derived from rat thymus nuclei labelled in vitro with [32P]phosphate.

Full text

PDF
509

Selected References

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

  1. ALLFREY V. G., LITTAU V. C., MIRSKY A. E. On the role of of histones in regulation ribonucleic acid synthesis in the cell nucleus. Proc Natl Acad Sci U S A. 1963 Mar 15;49:414–421. doi: 10.1073/pnas.49.3.414. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BARTLETT G. R. Phosphorus assay in column chromatography. J Biol Chem. 1959 Mar;234(3):466–468. [PubMed] [Google Scholar]
  3. BONNER J., HUANG R. C. Properties of chromosomal nucleohistone. J Mol Biol. 1963 Mar;6:169–174. doi: 10.1016/s0022-2836(63)80065-0. [DOI] [PubMed] [Google Scholar]
  4. Buckingham R. H., Stocken L. A. Fractionation of the lysine-rich histones. Biochem J. 1969 Oct;114(4):55P–55P. doi: 10.1042/bj1140055pa. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. DEAKIN H., ORD M. G., STOCKEN L. A. 'GLUCOSE 6-PHOSPHATE-DEHYDROGENASE' ACTIVITY AND THIOL CONTENT OF THYMUS NUCLEI FROM CONTROL AND X-IRRADIATED RATS. Biochem J. 1963 Nov;89:296–304. doi: 10.1042/bj0890296. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. HEILMANN J., BARROLLIER J., WATZKE E. Beitrag zur Aminosäurebestimmung auf Papierchromatogrammen. Hoppe Seylers Z Physiol Chem. 1957;309(4-6):219–220. [PubMed] [Google Scholar]
  8. HNILICA L. S., BUSCH H. Fractionation of the histones of the Walker 256 carcinosarcoma by combined chemical and chromatographic techniques. J Biol Chem. 1963 Mar;238:918–924. [PubMed] [Google Scholar]
  9. Hnilica L. S. Studies on nuclear proteins. I. Observations on the tissue and species specificity of the moderately lysine-rich histone fraction 2b. Biochim Biophys Acta. 1966 Mar 28;117(1):163–175. doi: 10.1016/0304-4165(66)90163-2. [DOI] [PubMed] [Google Scholar]
  10. Johns E. W. Studies on histones. 7. Preparative methods for histone fractions from calf thymus. Biochem J. 1964 Jul;92(1):55–59. doi: 10.1042/bj0920055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. KLOUWEN H. M., BETEL I. RADIOSENSITIVITY OF NUCLEAR ATP-SYNTHESIS. Int J Radiat Biol Relat Stud Phys Chem Med. 1963 May;6:441–461. doi: 10.1080/09553006314550541. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Langan T. A. Histone phosphorylation: stimulation by adenosine 3',5'-monophosphate. Science. 1968 Nov 1;162(3853):579–580. doi: 10.1126/science.162.3853.579. [DOI] [PubMed] [Google Scholar]
  14. Laurence D. J., Phillips D. M., Butler J. A. A comparison of histone fractions from an "osteogenic" rat tumor and calf thymus. Arch Biochem Biophys. 1966 Feb;113(2):338–346. doi: 10.1016/0003-9861(66)90195-0. [DOI] [PubMed] [Google Scholar]
  15. Laurence D. J., Simson P., Butler J. A. Studies on histones. 5. The histones of the Crocker sarcoma and spontaneous mammary tumours of mice. Biochem J. 1963 Apr;87(1):200–205. doi: 10.1042/bj0870200. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ord M. G., Stocken L. A. Metabolic properties of histones from rat liver and thymus gland. Biochem J. 1966 Mar;98(3):888–897. doi: 10.1042/bj0980888. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ord M. G., Stocken L. A. Variations in the phosphate content and thiołdisulphide ratio of histones during the cell cycle. Studies with regenerating rat liver and sea urchins. Biochem J. 1968 Apr;107(3):403–410. doi: 10.1042/bj1070403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. PHILLIPS D. M. The presence of acetyl groups of histones. Biochem J. 1963 May;87:258–263. doi: 10.1042/bj0870258. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Pogo B. G., Allfrey V. G., Mirsky A. E. RNA synthesis and histone acetylation during the course of gene activation in lymphocytes. Proc Natl Acad Sci U S A. 1966 Apr;55(4):805–812. doi: 10.1073/pnas.55.4.805. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Pogo B. G., Pogo A. O., Allfrey V. G., Mirsky A. E. Changing patterns of histone acetylation and RNA synthesis in regeneration of the liver. Proc Natl Acad Sci U S A. 1968 Apr;59(4):1337–1344. doi: 10.1073/pnas.59.4.1337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. REISFELD R. A., LEWIS U. J., WILLIAMS D. E. Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature. 1962 Jul 21;195:281–283. doi: 10.1038/195281a0. [DOI] [PubMed] [Google Scholar]
  22. Stellwagen R. H., Cole R. D. Comparsion of histones obtained from mammary gland at different stages of development and lactation. J Biol Chem. 1968 Sep 10;243(17):4456–4462. [PubMed] [Google Scholar]
  23. Stevely W. S., Stocken L. A. Variations in the phosphate content of histone F1 in normal and irradiated tissues. Biochem J. 1968 Nov;110(2):187–191. doi: 10.1042/bj1100187. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES