Skip to main content
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
. 1968 Oct;61(2):629–635. doi: 10.1073/pnas.61.2.629

Reversible changes of ordered polypeptide structures in oxidized and reduced epimerase.

A U Bertland 2nd, H M Kalckar
PMCID: PMC225206  PMID: 5245995

Full text

PDF
629

Selected References

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

  1. Atassi M. Z., Cacciotti L. R. Infra-red spectral analysis of the apoproteins of some haemoglobins and myoglobins. Nature. 1966 Mar 19;209(5029):1211–1213. doi: 10.1038/2091211a0. [DOI] [PubMed] [Google Scholar]
  2. BRESLOW E., BEYCHOK S., HARDMAN K. D., GURD F. R. RELATIVE CONFORMATIONS OF SPERM WHALE METMYOGLOBIN AND APOMYOGLOBIN IN SOLUTION. J Biol Chem. 1965 Jan;240:304–309. [PubMed] [Google Scholar]
  3. Beychok S. Rotatory dispersion and circular dichroism. Annu Rev Biochem. 1968;37:437–462. doi: 10.1146/annurev.bi.37.070168.002253. [DOI] [PubMed] [Google Scholar]
  4. Bolton W., Cox J. M., Perutz M. F. Structure and function of haemoglobin. IV. A three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5 A resolution. J Mol Biol. 1968 Apr 14;33(1):283–297. doi: 10.1016/0022-2836(68)90294-5. [DOI] [PubMed] [Google Scholar]
  5. Creveling C. R., Bhaduri A., Christensen A., Kalckar H. M. Molecular transitions in an induced enzyme with enhanced fluorescence. Biochem Biophys Res Commun. 1965 Dec 21;21(6):624–630. doi: 10.1016/0006-291x(65)90532-2. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Darrow R. A., Rodstrom R. Purification and properties of uridine diphosphate galactose 4-epimerase from yeast. Biochemistry. 1968 May;7(5):1645–1654. doi: 10.1021/bi00845a005. [DOI] [PubMed] [Google Scholar]
  8. Darrow R. A., Rodstrom R. Subunit association and catalytic activity of uridine diphosphate galactose-4-epimerase from yeast. Proc Natl Acad Sci U S A. 1966 Jan;55(1):205–212. doi: 10.1073/pnas.55.1.205. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. HARRISON S. C., BLOUT E. R. REVERSIBLE CONFORMATIONAL CHANGES OF MYOGLOBIN AND APOMYOGLOBIN. J Biol Chem. 1965 Jan;240:299–303. [PubMed] [Google Scholar]
  11. Sarkar P. K., Doty P. The optical rotatory properties of the beta-configuration in polypeptides and proteins. Proc Natl Acad Sci U S A. 1966 Apr;55(4):981–989. doi: 10.1073/pnas.55.4.981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Townend R., Kumosinski T. F., Timasheff S. N., Fasman G. D., Davidson B. The circular dichroism of the beta structure of poly-L-lysine. Biochem Biophys Res Commun. 1966 Apr 19;23(2):163–169. doi: 10.1016/0006-291x(66)90522-5. [DOI] [PubMed] [Google Scholar]
  13. ULMER D. D. OPTICAL ROTATORY DISPERSION OF OXIDIZED AND REDUCED CYTOCHROME C. Biochemistry. 1965 May;4:902–907. doi: 10.1021/bi00881a017. [DOI] [PubMed] [Google Scholar]
  14. Ulmer D. D., Vallee B. L. Extrinsic cotton effects and the mechanism of enzyme action. Adv Enzymol Relat Areas Mol Biol. 1965;27:37–104. doi: 10.1002/9780470122723.ch2. [DOI] [PubMed] [Google Scholar]
  15. Urry D. W. The heme chromophore in the ultraviolet. J Biol Chem. 1967 Oct 10;242(19):4441–4448. [PubMed] [Google Scholar]
  16. Vinogradov S., Zand R. Circular dichroism studies. I. Cytochrome c. Arch Biochem Biophys. 1968 Jun;125(3):902–910. doi: 10.1016/0003-9861(68)90529-8. [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