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. 1961 Oct;47(10):1530–1547. doi: 10.1073/pnas.47.10.1530

THE INACTIVATION OF TRYPSIN BY ULTRAVIOLET LIGHT, I. THE CORRELATION OF INACTIVATION WITH THE DISRUPTION OF CONSTITUENT CYSTINE*,a

L G Augenstine 1, C A Ghiron 1
PMCID: PMC223172  PMID: 13863246

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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. AROSKAR J. P., DICKMAN S. R., KROPF R. B. Activation and inhibition of beef pancreas ribonuclease. Biochim Biophys Acta. 1956 Sep;21(3):539–545. doi: 10.1016/0006-3002(56)90192-5. [DOI] [PubMed] [Google Scholar]
  3. AUGENSTINE L. Structural correlation between esterase and protease activities on trypsin. Science. 1959 Mar 13;129(3350):718–719. doi: 10.1126/science.129.3350.718. [DOI] [PubMed] [Google Scholar]
  4. CECIL R., McPHEE J. R. The sulfur chemistry of proteins. Adv Protein Chem. 1959;14:255–389. doi: 10.1016/s0065-3233(08)60613-0. [DOI] [PubMed] [Google Scholar]
  5. CUNNINGHAM L. W., Jr Molecular-kinetic properties of crystalline diisopropyl phosphoryl trypsin. J Biol Chem. 1954 Nov;211(1):13–19. [PubMed] [Google Scholar]
  6. GLAZER A. N., SMITH E. L. Estimation of cystine plus cysteine in proteins by the disulfide interchange reaction. J Biol Chem. 1961 Feb;236:416–421. [PubMed] [Google Scholar]
  7. Galston A. W., Baker R. S. Inactivation of Enzymes by Visible Light in the Presence of Riboflavin. Science. 1949 May 13;109(2837):485–486. doi: 10.1126/science.109.2837.485. [DOI] [PubMed] [Google Scholar]
  8. HUGGINS C., TAPLEY D. F., JENSEN E. V. Sulphydryl-disulphide relationships in the induction of gels in proteins by urea. Nature. 1951 Apr 14;167(4250):592–593. doi: 10.1038/167592a0. [DOI] [PubMed] [Google Scholar]
  9. JANSEN E. F., BALLS A. K. The inhibition of beta- and gamma-chymotrypsin and trypsin by diisopropyl fluorophosphate. J Biol Chem. 1952 Feb;194(2):721–727. [PubMed] [Google Scholar]
  10. JENSEN E. V. Sulfhydryl-disulfide interchange. Science. 1959 Nov 13;130(3385):1319–1323. doi: 10.1126/science.130.3385.1319. [DOI] [PubMed] [Google Scholar]
  11. KOSHLAND D. E., Jr, RAY W. J., Jr, ERWIN M. J. Protein structure and enzyme action. Fed Proc. 1958 Dec;17(4):1145–1150. [PubMed] [Google Scholar]
  12. LIENER I. E. The essentiality of the disulfide linkages in trypsin. J Biol Chem. 1957 Apr;225(2):1061–1069. [PubMed] [Google Scholar]
  13. MCLAREN A. D. Photochemistry of proteins XVIII. Some observations with enzymes and nucleic acids, and discussion. Enzymologia. 1957 Jan 30;18(2):81–96. [PubMed] [Google Scholar]
  14. OTEY M. C., GREENSTEIN J. P. Studies on polycysteine peptides and proteins. II. Apparent dissociation constants, and ultra-violet and infrared absorption spectra of isomeric cystinylcystine peptides. Arch Biochem Biophys. 1954 Dec;53(2):501–513. doi: 10.1016/0003-9861(54)90432-4. [DOI] [PubMed] [Google Scholar]
  15. RAY W. J., Jr, KOSHLAND D. E., Jr Comparative structural studies of phosphoglucomutase and chymotrypsin. Brookhaven Symp Biol. 1960 Nov;13:135–150. [PubMed] [Google Scholar]
  16. RYLE A. P., SANGER F. Disulphide interchange reactions. Biochem J. 1955 Aug;60(4):535–540. [PMC free article] [PubMed] [Google Scholar]
  17. SETLOW R., DOYLE B. The action of monochromatic ultraviolet light on proteins. Biochim Biophys Acta. 1957 Apr;24(1):27–41. doi: 10.1016/0006-3002(57)90142-7. [DOI] [PubMed] [Google Scholar]
  18. SPACKMAN D. H., STEIN W. H., MOORE S. The disulfide bonds of ribonuclease. J Biol Chem. 1960 Mar;235:648–659. [PubMed] [Google Scholar]
  19. STRYER L. Energy transfer in proteins and polypeptides. Radiat Res. 1960;Suppl 2:432–451. [PubMed] [Google Scholar]
  20. WEIL L., JAMES S., BUCHERT A. R. Photo-oxidation of crystalline chymotrypsin in the presence of methylene blue. Arch Biochem Biophys. 1953 Oct;46(2):266–278. doi: 10.1016/0003-9861(53)90200-8. [DOI] [PubMed] [Google Scholar]
  21. WHITE F. H., Jr Regeneration of enzymatic activity by airoxidation of reduced ribonuclease with observations on thiolation during reduction with thioglycolate. J Biol Chem. 1960 Feb;235:383–389. [PubMed] [Google Scholar]

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