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. 1981 Jan;78(1):192–195. doi: 10.1073/pnas.78.1.192

Purification of thymus mRNA coding for a 16,000-dalton polypeptide containing the thymosin alpha 1 sequence.

M Freire, E Hannappel, M Rey, J M Freire, H Kido, B L Horecker
PMCID: PMC319017  PMID: 6941243

Abstract

A mRNA fraction purified by preparative polyacrylamide disc gel electrophoresis from calf thymus polysomes codes for a polypeptide(s) having a mass of 16,000-17,000 daltons. This polypeptide contains amino acid sequences corresponding to residues 11-18 and 19-25 of thymosin alpha 1. The yield of the octapeptide indicates that the 16,000-dalton peptide is the major product formed in the cell-free synthesis system containing the purified mRNA.

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Selected References

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

  1. Böhlen P., Stein S., Stone J., Udenfriend S. Automatic Monitoring of primary amines in preparative column effluents with fluorescamine. Anal Biochem. 1975 Aug;67(2):438–445. doi: 10.1016/0003-2697(75)90316-4. [DOI] [PubMed] [Google Scholar]
  2. Drapeau G. R. Cleavage at glutamic acid with staphylococcal protease. Methods Enzymol. 1977;47:189–191. doi: 10.1016/0076-6879(77)47023-x. [DOI] [PubMed] [Google Scholar]
  3. Freire M., Crivellaro O., Isaacs C., Moschera J., Horecker B. L. Translation of mRNA from calf thymus in the wheat germ system: evidence for a precursor of thymosin alpha1. Proc Natl Acad Sci U S A. 1978 Dec;75(12):6007–6011. doi: 10.1073/pnas.75.12.6007. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Goldstein A. L., Low T. L., McAdoo M., McClure J., Thurman G. B., Rossio J., Lai C. Y., Chang D., Wang S. S., Harvey C. Thymosin alpha1: isolation and sequence analysis of an immunologically active thymic polypeptide. Proc Natl Acad Sci U S A. 1977 Feb;74(2):725–729. doi: 10.1073/pnas.74.2.725. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Loening U. E. The fractionation of high-molecular-weight ribonucleic acid by polyacrylamide-gel electrophoresis. Biochem J. 1967 Jan;102(1):251–257. doi: 10.1042/bj1020251. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Low T. L., Thurman G. B., McAdoo M., McClure J., Rossio J. L., Naylor P. H., Goldstein A. L. The chemistry and biology of thymosin. I. Isolation, characterization, and biological activities of thymosin alpha1 and polypeptide beta1 from calf thymus. J Biol Chem. 1979 Feb 10;254(3):981–986. [PubMed] [Google Scholar]
  7. Palmiter R. D. Magnesium precipitation of ribonucleoprotein complexes. Expedient techniques for the isolation of undergraded polysomes and messenger ribonucleic acid. Biochemistry. 1974 Aug 13;13(17):3606–3615. doi: 10.1021/bi00714a032. [DOI] [PubMed] [Google Scholar]
  8. Pinder J. C., Staynov D. Z., Gratzer W. B. Electrophoresis of RNA in formamide. Biochemistry. 1974 Dec 17;13(26):5373–5378. doi: 10.1021/bi00723a019. [DOI] [PubMed] [Google Scholar]
  9. Rubinstein M. Preparative high-performance liquid partition chromatography of proteins. Anal Biochem. 1979 Sep 15;98(1):1–7. doi: 10.1016/0003-2697(79)90697-3. [DOI] [PubMed] [Google Scholar]

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