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. 1985 Nov;48(5):799–802. doi: 10.1016/S0006-3495(85)83838-8

The effect of iron binding on the conformation of transferrin. A small angle x-ray scattering study.

F Kilár, I Simon
PMCID: PMC1329405  PMID: 4074838

Abstract

Distance distribution functions, p(r), radii of gyration, Rg, and radii of gyration of cross section, Rq, of apotransferrin, monoferric transferrin, and diferric transferrin have been compared. The alteration of Rg and Rq upon iron binding has been determined by a difference method. An unusual feature of the stepwise structural changes of transferrin upon iron saturation is that binding of the first ferric ion is responsible for more than half of the whole change in Rq, whereas Rg alters significantly only after the binding of the second ferric ion.

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Selected References

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

  1. Aisen P., Leibman A., Zweier J. Stoichiometric and site characteristics of the binding of iron to human transferrin. J Biol Chem. 1978 Mar 25;253(6):1930–1937. [PubMed] [Google Scholar]
  2. Bates G. W., Schlabach M. R. The reaction of ferric salts with transferrin. J Biol Chem. 1973 May 10;248(9):3228–3232. [PubMed] [Google Scholar]
  3. Brock J. H., Arzabe F., Lampreave F., Piñeiro A. The effect of trypsin on bovine transferrin and lactoferrin. Biochim Biophys Acta. 1976 Sep 28;446(1):214–225. doi: 10.1016/0005-2795(76)90112-4. [DOI] [PubMed] [Google Scholar]
  4. DeLucas L. J., Suddath F. L., Gams R. A., Bugg C. E. Preliminary x-ray study of crystals of human transferrin. J Mol Biol. 1978 Aug 5;123(2):285–286. doi: 10.1016/0022-2836(78)90328-5. [DOI] [PubMed] [Google Scholar]
  5. Evans R. W., Williams J. Studies of the binding of different iron donors to human serum transferrin and isolation of iron-binding fragments from the N- and C-terminal regions of the protein. Biochem J. 1978 Aug 1;173(2):543–552. doi: 10.1042/bj1730543. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gorinsky B., Horsburgh C., Lindley P. F., Moss D. S., Parkar M., Watson J. L. Evidence for the bilobal nature of diferric rabbit plasma transferrin. Nature. 1979 Sep 13;281(5727):157–158. doi: 10.1038/281157a0. [DOI] [PubMed] [Google Scholar]
  7. Kilár F., Simon I., Lakatos S., Vonderviszt F., Medgyesi G. A., Závodszky P. Conformation of human IgG subclasses in solution. Small-angle X-ray scattering and hydrodynamic studies. Eur J Biochem. 1985 Feb 15;147(1):17–25. doi: 10.1111/j.1432-1033.1985.tb08712.x. [DOI] [PubMed] [Google Scholar]
  8. Makey D. G., Seal U. S. The detection of four molecular forms of human transferrin during the iron binding process. Biochim Biophys Acta. 1976 Nov 26;453(1):250–256. doi: 10.1016/0005-2795(76)90270-1. [DOI] [PubMed] [Google Scholar]
  9. Martel P., Kim S. M., Powell B. M. Physical characteristics of human transferrin from small angle neutron scattering. Biophys J. 1980 Sep;31(3):371–380. doi: 10.1016/S0006-3495(80)85065-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Pilz I., Glatter O., Kratky O. Small-angle X-ray scattering. Methods Enzymol. 1979;61:148–249. doi: 10.1016/0076-6879(79)61013-3. [DOI] [PubMed] [Google Scholar]
  11. Rosseneu-Motreff M. Y., Soetewey F., Lamote R., Peeters H. Size and shape determination of apotransferrin and transferrin monomers. Biopolymers. 1971 Jun;10(6):1039–1048. doi: 10.1002/bip.360100610. [DOI] [PubMed] [Google Scholar]
  12. Simon I., Móra S., Elödi P. Studies on the active center of pancreatic amylase. II. Small angle x-ray scattering investigations. Mol Cell Biochem. 1974 Oct 30;4(3):211–216. doi: 10.1007/BF01731483. [DOI] [PubMed] [Google Scholar]
  13. Simon I. Study of the position of NAD and its effect on the conformation of D-glyceraldehyde-3-phosphate dehydrogenase by small-angle x-ray scattering. Eur J Biochem. 1972 Oct 17;30(1):184–189. doi: 10.1111/j.1432-1033.1972.tb02085.x. [DOI] [PubMed] [Google Scholar]
  14. Stamatoff J. An approach for time-resolved x-ray scattering. Biophys J. 1979 May;26(2):325–327. doi: 10.1016/S0006-3495(79)85252-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Yeh S. M., Meares C. F. Characterization of transferrin metal-binding sites by diffusion-enhanced energy transfer. Biochemistry. 1980 Oct 28;19(22):5057–5062. doi: 10.1021/bi00563a019. [DOI] [PubMed] [Google Scholar]

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