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. 1973 Sep;135(1):87–92. doi: 10.1042/bj1350087

Structural studies on individual components of bovine transferrin

N E Richardson 1,2, N Buttress 1,2, A Feinstein 1,2, A Stratil 1,2,*, R L Spooner 1,2
PMCID: PMC1165792  PMID: 4798182

Abstract

The single-banding components of bovine transferrin from animals homozygous for the four transferrin variants found in the U.K. were isolated. Sedimentation equilibrium ultracentrifugation and sodium dodecyl sulphate–polyacrylamide-gel electrophoresis showed that the bands of a single variant have molecular weights of 77500 and 73300 respectively. The different bands of a single variant and single bands of different variants show no evidence of size heterogeneity or of low-molecular-weight peptides being split off after reduction in 6m-guanidine hydrochloride. The two slower bands of a single variant, which both contain 2 molecules of sialic acid/molecule of protein, have the same molecular weight and amino acid composition, and give identical peptide `maps', although differences in composition and peptide `maps' occur between the different variants. The results support the concept that bovine transferrin is essentially a single polypeptide chain, but they do not explain differences in electrophoretic mobility between bands of the same variant which are not produced by differing sialic acid content.

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Selected References

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

  1. Beale D., Feinstein A. Studies on the reduction of a human 19S immunoglobulin M. Biochem J. 1969 Apr;112(2):187–194. doi: 10.1042/bj1120187. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bezkorovainy A., Grohlich D., Gerbeck C. M. Some physical-chemical properties of reduced-alkylated and sulphitolysed human serum transferrins and hen's-egg conalbumin. Biochem J. 1968 Dec;110(4):765–770. doi: 10.1042/bj1100765. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bezkorovainy A., Grohlich D. The behavior of nativ and reduced-alkylated human transferrin in urea and guanidine-HCl solutions. Biochim Biophys Acta. 1967 Dec 12;147(3):497–510. doi: 10.1016/0005-2795(67)90009-8. [DOI] [PubMed] [Google Scholar]
  4. Greene F. C., Feeney R. E. Physical evidence for transferrins as single polypeptide chains. Biochemistry. 1968 Apr;7(4):1366–1371. doi: 10.1021/bi00844a018. [DOI] [PubMed] [Google Scholar]
  5. Hade E. P., Tanford C. Isopiestic compositions as a measure of preferential interactions of macromolecules in two-component solvents. Application to proteins in concentrated aqueous cesium chloride and guanidine hydrochloride. J Am Chem Soc. 1967 Sep 13;89(19):5034–5040. doi: 10.1021/ja00995a036. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Jeppsson J. O. Subunits of human transferrin. Acta Chem Scand. 1967;21(7):1686–1694. doi: 10.3891/acta.chem.scand.21-1686. [DOI] [PubMed] [Google Scholar]
  8. Mann K. G., Fish W. W., Cox A. C., Tanford C. Single-chain nature of human serum transferrin. Biochemistry. 1970 Mar 17;9(6):1348–1354. doi: 10.1021/bi00808a008. [DOI] [PubMed] [Google Scholar]
  9. Palmour R. M., Sutton H. E. Vertebrae transferrins. Molecular weights, chemical compositions, and iron-binding studies. Biochemistry. 1971 Oct 26;10(22):4026–4032. doi: 10.1021/bi00798a003. [DOI] [PubMed] [Google Scholar]
  10. SCHEIDEGGER J. J. Une micro-méthode de l'immuno-electrophorèse. Int Arch Allergy Appl Immunol. 1955;7(2):103–110. [PubMed] [Google Scholar]
  11. Spooner R. L., Baxter G. Abnormal expression of normal transferrin alleles in cattle. Biochem Genet. 1969 Jan;2(4):371–382. doi: 10.1007/BF01458497. [DOI] [PubMed] [Google Scholar]
  12. Stratil A., Spooner R. L. Isolation and properties of individual components of cattle transferrin: the role of sialic acid. Biochem Genet. 1971 Aug;5(4):347–365. doi: 10.1007/BF00485861. [DOI] [PubMed] [Google Scholar]
  13. Summers D. F., Maizel J. V., Jr, Darnell J. E., Jr Evidence for virus-specific noncapsid proteins in poliovirus-infected HeLa cells. Proc Natl Acad Sci U S A. 1965 Aug;54(2):505–513. doi: 10.1073/pnas.54.2.505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. YPHANTIS D. A. EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS. Biochemistry. 1964 Mar;3:297–317. doi: 10.1021/bi00891a003. [DOI] [PubMed] [Google Scholar]

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