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. 1968 Apr;59(4):1321–1328. doi: 10.1073/pnas.59.4.1321

The amino acid sequence of porcine thyrocalcitonin.

J T Potts Jr, H D Niall, H T Keutmann, H B Brewer Jr, L J Deftos
PMCID: PMC224870  PMID: 5240032

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Selected References

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

  1. ANFINSEN C. B., HABER E. Studies on the reduction and re-formation of protein disulfide bonds. J Biol Chem. 1961 May;236:1361–1363. [PubMed] [Google Scholar]
  2. Benisek W. F., Cole R. D. Sodium/liquid ammonia reduction of proline-containing peptides. Biochem Biophys Res Commun. 1965 Sep 8;20(5):655–660. doi: 10.1016/0006-291x(65)90451-1. [DOI] [PubMed] [Google Scholar]
  3. Benson J. V., Jr, Jones R. T., Cormick J., Patterson J. A. Accelerated automatic chromatographic analysis of peptides on a spherical resin. Anal Biochem. 1966 Jul;16(1):91–106. doi: 10.1016/0003-2697(66)90084-4. [DOI] [PubMed] [Google Scholar]
  4. Copp D. H. Hormonal control of hypercalcemia. Historic development of the calcitonin concept. Am J Med. 1967 Nov;43(5):648–655. doi: 10.1016/0002-9343(67)90105-2. [DOI] [PubMed] [Google Scholar]
  5. EDMAN P. Phenylthiohydantoins in protein analysis. Ann N Y Acad Sci. 1960 Aug 31;88:602–610. doi: 10.1111/j.1749-6632.1960.tb20056.x. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Edman P., Begg G. A protein sequenator. Eur J Biochem. 1967 Mar;1(1):80–91. doi: 10.1007/978-3-662-25813-2_14. [DOI] [PubMed] [Google Scholar]
  8. HIRS C. H. The oxidation of ribonuclease with performic acid. J Biol Chem. 1956 Apr;219(2):611–621. [PubMed] [Google Scholar]
  9. Hubbard R. W., Kremen D. M. Increased sensitivity of accelerated amino acid ion-exchange chromatography. Anal Biochem. 1965 Sep;12(3):593–602. doi: 10.1016/0003-2697(65)90227-7. [DOI] [PubMed] [Google Scholar]
  10. Hubbard R. W. Studies in accelerated amino acid analysis. Biochem Biophys Res Commun. 1965 Jun 9;19(6):679–685. doi: 10.1016/0006-291x(65)90310-4. [DOI] [PubMed] [Google Scholar]
  11. Munson P. L., Hirsch P. F. Discovery and pharmacologic evaluation of thyrocalcitonin. Am J Med. 1967 Nov;43(5):678–683. doi: 10.1016/0002-9343(67)90109-x. [DOI] [PubMed] [Google Scholar]
  12. POTTS J. T., BERGER A., COOKE J., ANFINSEN C. B. A reinvestigation of the sequence of residues 11 to 18 in bovine pancreatic ribonuclease. J Biol Chem. 1962 Jun;237:1851–1855. [PubMed] [Google Scholar]
  13. Potts J. T., Jr, Reisfeld R. A., Hirsch P. F., Wasthed A. B., Voelkel E. F., Munson P. L. Purification of porcine thyrocalcitonin. Proc Natl Acad Sci U S A. 1967 Jul;58(1):328–335. doi: 10.1073/pnas.58.1.328. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Putter I., Kaczka E. A., Harman R. E., Rickes E. L., Kempf A. J., Chaiet L., Rothrock J. W., Wase A. W., Wolf F. J. The isolation and properties of thyrocalcitonin. J Am Chem Soc. 1967 Sep 27;89(20):5301–5302. [PubMed] [Google Scholar]

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