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. 1982 Sep 1;205(3):611–617. doi: 10.1042/bj2050611

The preparation and partial characterization of N-terminal and C-terminal iron-binding fragments from rabbit serum transferrin.

S Heaphy, J Williams
PMCID: PMC1158528  PMID: 6816218

Abstract

Two iron-binding fragments of Mr 36 000 and 33 000 corresponding to the N-terminal domain of rabbit serum transferrin were prepared. One iron-binding fragment of Mr 39 000 corresponding to the C-terminal domain was prepared. The N-terminal amino acid sequence of rabbit serum transferrin is: Val-Thr-Glu-Lys-Thr-Val-Asn-Trp-?-Ala-Val-Ser. One glycan unit is presented in rabbit serum transferrin and it is located in the C-terminal domain.

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Selected References

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  1. Baker E., Shaw D. C., Morgan E. H. Isolation and characterization of rabbit serum and milk transferrins. Evidence for difference in sialic acid content only. Biochemistry. 1968 Apr;7(4):1371–1378. doi: 10.1021/bi00844a019. [DOI] [PubMed] [Google Scholar]
  2. Bluard-Deconinck J. M., Williams J., Evans R. W., van Snick J., Osinski P. A., Masson P. L. Iron-binding fragments from the N-terminal and C-terminal regions of human lactoferrin. Biochem J. 1978 May 1;171(2):321–327. doi: 10.1042/bj1710321. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brock J. H., Arzabe F. R. Cleavage of differic bovine transferrin into two monoferric fragments. FEBS Lett. 1976 Oct 15;69(1):63–66. doi: 10.1016/0014-5793(76)80654-0. [DOI] [PubMed] [Google Scholar]
  4. CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
  5. Chasteen N. D., Williams J. The influence of pH on the equilibrium distribution of iron between the metal-binding sites of human transferrin. Biochem J. 1981 Mar 1;193(3):717–727. doi: 10.1042/bj1930717. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dorland L., Haverkamp J., Vliegenthart J. F., Spik G., Fournet B., Montreuil J. Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy and methylation analysis of the single glycan chain of chicken ovotransferrin. Eur J Biochem. 1979 Oct 15;100(2):569–574. doi: 10.1111/j.1432-1033.1979.tb04203.x. [DOI] [PubMed] [Google Scholar]
  7. Esparza I., Brock J. H. The effect of trypsin digestion on the structure and iron-donating properties of transferrins from several species. Biochim Biophys Acta. 1980 Apr 25;622(2):297–307. doi: 10.1016/0005-2795(80)90040-9. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. 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]
  10. Groen R., Hendricksen P., Young S. P., Leibman A., Aisen P. Molecular ferrokinetics in the rabbit. Br J Haematol. 1982 Jan;50(1):43–53. doi: 10.1111/j.1365-2141.1982.tb01889.x. [DOI] [PubMed] [Google Scholar]
  11. Harris D. C., Aisen P. Functional equivalence of the two iron-binding sites of human transferrin. Nature. 1975 Oct 30;257(5529):821–823. doi: 10.1038/257821a0. [DOI] [PubMed] [Google Scholar]
  12. Harris D. C., Aisen P. Iron-donating properties of transferrin. Biochemistry. 1975 Jan 28;14(2):262–268. doi: 10.1021/bi00673a011. [DOI] [PubMed] [Google Scholar]
  13. Hudson B. G., Ono M., Brockway W. J., Castellino F. J. Chemical and physical properties of serum transferrins from several species. Biochemistry. 1973 Mar 13;12(6):1047–1053. doi: 10.1021/bi00730a005. [DOI] [PubMed] [Google Scholar]
  14. JAMIESON G. A. STUDIES ON GLYCOPROTEINS. II. ISOLATION OF THE CARBOHYDRATE CHAINS OF HUMAN TRANSFERRIN. J Biol Chem. 1965 Jul;240:2914–2920. [PubMed] [Google Scholar]
  15. Leger D., Tordera V., Spik G., Dorland L., Haverkamp J., Vliegenthart J. F. Structure determination of the single glycan of rabbit serotransferrin by methylation analysis and 360 MHz 1H NMR spectroscopy. FEBS Lett. 1978 Sep 15;93(2):255–260. doi: 10.1016/0014-5793(78)81116-8. [DOI] [PubMed] [Google Scholar]
  16. Lineback-Zins J., Brew K. Preparation and characterization of an NH2-terminal fragment of human serum transferrin containing a single iron-binding site. J Biol Chem. 1980 Jan 25;255(2):708–713. [PubMed] [Google Scholar]
  17. 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]
  18. Martinez-Medellin J., Schulman H. M. The kinetics of iron and transferrin incorporation into rabbit erythroid cells and the nature of stromal-bound iron. Biochim Biophys Acta. 1972 Apr 21;264(2):272–274. doi: 10.1016/0304-4165(72)90291-7. [DOI] [PubMed] [Google Scholar]
  19. Mendez E., Lai C. Y. Regeneration of amino acids from thiazolinones formed in the Edman degradation. Anal Biochem. 1975 Sep;68(1):47–53. doi: 10.1016/0003-2697(75)90677-6. [DOI] [PubMed] [Google Scholar]
  20. OUCHTERLONY O. Diffusion-in-gel methods for immunological analysis. Prog Allergy. 1958;5:1–78. [PubMed] [Google Scholar]
  21. Schreiber G., Dryburgh H., Millership A., Matsuda Y., Inglis A., Phillips J., Edwards K., Maggs J. The synthesis and secretion of rat transferrin. J Biol Chem. 1979 Dec 10;254(23):12013–12019. [PubMed] [Google Scholar]
  22. Spik G., Bayard B., Fournet B., Strecker G., Bouquelet S., Montreuil J. Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrin. FEBS Lett. 1975 Feb 15;50(3):296–299. doi: 10.1016/0014-5793(75)80513-8. [DOI] [PubMed] [Google Scholar]
  23. Strickland D. K., Hamilton J. W., Hudson B. G. Structure of the tryptic glycopeptide isolated from rabbit transferrin. Biochemistry. 1979 Jun 12;18(12):2549–2554. doi: 10.1021/bi00579a018. [DOI] [PubMed] [Google Scholar]
  24. Tsao D., Morris D. H., Azari P., Tengerdy R. P., Phillips J. L. On the structure of ovotransferrin. II. Isolation and characterization of a specific iron-binding fragment after cyanogen bromide cleavage. Biochemistry. 1974 Jan 29;13(3):403–407. doi: 10.1021/bi00700a002. [DOI] [PubMed] [Google Scholar]
  25. WARNER R. C., WEBER I. The preparation of crystalline conalbumin. J Biol Chem. 1951 Jul;191(1):173–180. [PubMed] [Google Scholar]
  26. WINZLER R. J. Determination of serum glycoproteins. Methods Biochem Anal. 1955;2:279–311. doi: 10.1002/9780470110188.ch10. [DOI] [PubMed] [Google Scholar]
  27. Williams J., Chasteen N. D., Moreton K. The effect of salt concentration on the iron-binding properties of human transferrin. Biochem J. 1982 Mar 1;201(3):527–532. doi: 10.1042/bj2010527. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Williams J. Iron-binding fragments from the carboxyl-terminal region of hen ovotransferrin. Biochem J. 1975 Jul;149(1):237–244. doi: 10.1042/bj1490237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Williams J. The formation of iron-binding fragments of hen ovotransferrin by limited proteolysis. Biochem J. 1974 Sep;141(3):745–752. doi: 10.1042/bj1410745. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Woods K. R., Wang K. T. Separation of dansyl-amino acids by polyamide layer chromatography. Biochim Biophys Acta. 1967 Feb 21;133(2):369–370. doi: 10.1016/0005-2795(67)90078-5. [DOI] [PubMed] [Google Scholar]
  31. van Baarlen J., Brouwer J. T., Leibman A., Aisen P. Evidence for the functional heterogeneity of the two sites of transferrin in vitro. Br J Haematol. 1980 Nov;46(3):417–426. doi: 10.1111/j.1365-2141.1980.tb05988.x. [DOI] [PubMed] [Google Scholar]
  32. van Eijk H. G., van Dijk J. P., van Noort W. L., Leijnse B., Monfoort C. H. Isolation and analysis of transferrins from different species. Scand J Haematol. 1972;9(3):267–270. doi: 10.1111/j.1600-0609.1972.tb00939.x. [DOI] [PubMed] [Google Scholar]

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