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. 1968 Dec;61(4):1478–1485. doi: 10.1073/pnas.61.4.1478

Suppression of hydrogen exchange in staphylococcal nuclease by ligands.

A N Schechter, L Morávek, C B Anfinsen
PMCID: PMC225280  PMID: 5249820

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Selected References

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

  1. Cuatrecasas P., Fuchs S., Anfinsen C. B. Catalytic properties and specificity of the extracellular nuclease of Staphylococcus aureus. J Biol Chem. 1967 Apr 10;242(7):1541–1547. [PubMed] [Google Scholar]
  2. DISABATO G., OTTESEN M. EFFECT OF COENZYMES ON THE HYDROGEN-DEUTERIUM EXCHANGE OF CHICKEN HEART LACTIC DEHYDROGENASE AS MEASURED BY INFRARED SPECTROPHOTOMETRY. Biochemistry. 1965 Mar;4:422–428. doi: 10.1021/bi00879a007. [DOI] [PubMed] [Google Scholar]
  3. DeLuca M., Marsh M. Conformational changes of luciferase during catalyses. Tritium-hydrogen exchange and optical rotation studies. Arch Biochem Biophys. 1967 Jul;121(1):233–240. doi: 10.1016/0003-9861(67)90029-x. [DOI] [PubMed] [Google Scholar]
  4. ENGLANDER S. W. A HYDROGEN EXCHANGE METHOD USING TRITIUM AND SEPHADEX: ITS APPLICATION TO RIBONUCLEASE. Biochemistry. 1963 Jul-Aug;2:798–807. doi: 10.1021/bi00904a030. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fuchs S., Cuatrecasas P., Anfinsen C. B. An improved method for the purification of staphylococcal nuclease. J Biol Chem. 1967 Oct 25;242(20):4768–4770. [PubMed] [Google Scholar]
  6. HVIDT A., KAEGI J. H., OTTESEN M. EFFECT OF OXIDIZED NICOTINAMIDE-ADENINE DINUCLEOTIDE ON HYDROGEN-DEUTERIUM EXCHANGE OF YEAST ALCOHOL DEHYDROGENASE AS MEASURED BY INFRARED SPECTROPHOTOMETRY. Biochim Biophys Acta. 1963 Sep 24;75:290–292. doi: 10.1016/0006-3002(63)90614-0. [DOI] [PubMed] [Google Scholar]
  7. HVIDT A., LINDERSTRØM-LANG K. Exchange of hydrogen atoms in insulin with deuterium atoms in aqueous solutions. Biochim Biophys Acta. 1954 Aug;14(4):574–575. doi: 10.1016/0006-3002(54)90241-3. [DOI] [PubMed] [Google Scholar]
  8. Hvidt A., Nielsen S. O. Hydrogen exchange in proteins. Adv Protein Chem. 1966;21:287–386. doi: 10.1016/s0065-3233(08)60129-1. [DOI] [PubMed] [Google Scholar]
  9. Kägi J. H., Ulmer D. D. Hydrogen-deuterium exchange of cytochrome c. II. Effect of pH. Biochemistry. 1968 Aug;7(8):2718–2723. doi: 10.1021/bi00848a004. [DOI] [PubMed] [Google Scholar]
  10. Praissman M., Rupley J. A. Comparison of proteinstructure in the crystal and in solution. 3. Tritium-hydrogen exchange of lysozyme and a lysozyme-saccharide complex. Biochemistry. 1968 Jun;7(6):2446–2450. doi: 10.1021/bi00846a053. [DOI] [PubMed] [Google Scholar]
  11. Schechter A. N., Epstein C. J. Spectral studies on the denaturation of myoglobin. J Mol Biol. 1968 Aug 14;35(3):567–589. doi: 10.1016/s0022-2836(68)80015-4. [DOI] [PubMed] [Google Scholar]
  12. Taniuchi H., Anfinsen C. B., Sodja A. Nuclease-T: an active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragments. Proc Natl Acad Sci U S A. 1967 Sep;58(3):1235–1242. doi: 10.1073/pnas.58.3.1235. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Taniuchi H., Anfinsen C. B., Sodja A. The amino acid sequence of an extracellular nuclease of Staphylococcus aureus. 3. Complete amino acid sequence. J Biol Chem. 1967 Oct 25;242(20):4752–4758. [PubMed] [Google Scholar]
  14. Taniuchi H., Anfinsen C. B. Steps in the formation of active derivatives of staphylococcal nuclease during trypsin digestion. J Biol Chem. 1968 Sep 25;243(18):4778–4786. [PubMed] [Google Scholar]

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