Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1978 Feb;75(2):823–827. doi: 10.1073/pnas.75.2.823

Thymic hormone-like restoration by human prealbumin of azathioprine sensitivity of spleen cells from thymectomized mice.

P Burton, S Iden, K Mitchell, A White
PMCID: PMC411349  PMID: 273245

Abstract

Gel filtration of fresh human serum revealed that over 95% of the thymic-hormone-like activity was present in the fraction representing the total albumin and prealbumin. Further studies demonstrated that the activity resided in the prealbumin fraction; albumin was inactive. Prealbumin was isolated from Cohn fraction IV-1 of pooled human plasma by extraction with aqueous buffer, fractionation with (NH4)2SO4, gel filtration on Sephadex G-150, and preparative disc gel electrophoresis. The final product was homogeneous by analytical gel electrophoresis was 40,000 times more active than the starting material in an azathioprine-sensitive rosette assay. Physical and chemical characterization studies showed that the isolated product was identical to authentic human plasma prealbumin. Isolation of the prealbumin fraction from sera of adult thymectomized mice revealed that the rosette activity was substantially lower than that isolated from sera of normal mice, suggesting a thymic dependence of the prealbumin activity. In vitro and in vivo bioassays of the fraction obtained prior to the final step of the purification procedure support the conclusion that prealbumin exhibits thymic hormone-like activity.

Full text

PDF
823

Images in this article

824Image
on p.824
825Image
on p.825
826Image
on p.826

Selected References

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

  1. Bach J. F., Dardenne M., Goldstein A. L., Guha A., White A. Appearance of T-cell markers in bone marrow rosette-forming cells after incubation with thymosin, a thymic hormone. Proc Natl Acad Sci U S A. 1971 Nov;68(11):2734–2738. doi: 10.1073/pnas.68.11.2734. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bach J. F., Dardenne M., Pleau J. M., Bach M. A. Isolation, biochemical characteristics, and biological activity of a circulating thymic hormone in the mouse and in the human. Ann N Y Acad Sci. 1975 Feb 28;249:186–210. doi: 10.1111/j.1749-6632.1975.tb29068.x. [DOI] [PubMed] [Google Scholar]
  3. Bach J. F., Dardenne M. Thymus dependency of rosette-forming cells: evidence for a circulating thymic hormone. Transplant Proc. 1972 Sep;4(3):345–350. [PubMed] [Google Scholar]
  4. Bach J., Bardenne M., Pleau J., Rosa J. Biochemical characterisation of a serum thymic factor. Nature. 1977 Mar 3;266(5597):55–57. doi: 10.1038/266055a0. [DOI] [PubMed] [Google Scholar]
  5. Catsimpoolas N. Micro isoelectric focusing in polyacrylamide gel columns. Anal Biochem. 1968 Dec;26(3):480–482. doi: 10.1016/0003-2697(68)90219-4. [DOI] [PubMed] [Google Scholar]
  6. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  7. Goldstein A. L., Guha A., Zatz M. M., Hardy M. A., White A. Purification and biological activity of thymosin, a hormone of the thymus gland. Proc Natl Acad Sci U S A. 1972 Jul;69(7):1800–1803. doi: 10.1073/pnas.69.7.1800. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Goldstein A. L., Slater F. D., White A. Preparation, assay, and partial purification of a thymic lymphocytopoietic factor (thymosin). Proc Natl Acad Sci U S A. 1966 Sep;56(3):1010–1017. doi: 10.1073/pnas.56.3.1010. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hanlon D. P., De Vore L., Kincaid M. C., Jones A., Lane L. Thyroxine-binding prealbumin. Conformation in aqueous solutions. J Biol Chem. 1971 Oct 10;246(19):6011–6018. [PubMed] [Google Scholar]
  10. 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]
  11. Raz A., Shiratori T., Goodman D. S. Studies on the protein-protein and protein-ligand interactions involved in retinol transport in plasma. J Biol Chem. 1970 Apr 25;245(8):1903–1912. [PubMed] [Google Scholar]
  12. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  13. Weiner A. M., Platt T., Weber K. Amino-terminal sequence analysis of proteins purified on a nanomole scale by gel electrophoresis. J Biol Chem. 1972 May 25;247(10):3242–3251. [PubMed] [Google Scholar]
  14. White A., Goldstein A. L. The endocrine role of the thymus and its hormone, thymosin, in the regulation of the growth and maturation of host immunological competence. Adv Metab Disord. 1975;8:359–374. doi: 10.1016/b978-0-12-027308-9.50028-7. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES