The effect of pH upon human transferrin: selective labelling of the two iron-binding sites - PubMed (original) (raw)
The effect of pH upon human transferrin: selective labelling of the two iron-binding sites
A N Lestas. Br J Haematol. 1976 Mar.
Abstract
The influence of pH changes upon the iron-binding properties of transferrin was investigated in the absence of chelating agents. The effects were demonstrated by spectrophotometry, gel filtration, and by studies of the intermolecular transfer of 59Fe from transferrin to conalbumin. At pH values below 6.7, diferric transferrin readily loses iron. The monoferric molecule, which is relatively resistant to acid dissociation, is preferentially formed. A temporary reduction of pH provides a simple method for selectively attaching iron to one metal-binding site, and allows double isotopic labelling of the transferrin molecule. This technique may permit further investigation of the physiological properties of the two iron-binding sites.
Similar articles
- The influence of pH on the equilibrium distribution of iron between the metal-binding sites of human transferrin.
Chasteen ND, Williams J. Chasteen ND, et al. Biochem J. 1981 Mar 1;193(3):717-27. doi: 10.1042/bj1930717. Biochem J. 1981. PMID: 7305958 Free PMC article. - Metalloprotein analysis by capillary isoelectric focusing.
Richards MP, Huang TL. Richards MP, et al. J Chromatogr B Biomed Sci Appl. 1997 Mar 7;690(1-2):43-54. doi: 10.1016/s0378-4347(96)00407-0. J Chromatogr B Biomed Sci Appl. 1997. PMID: 9106028 - The iron-binding properties of hen ovotransferrin.
Williams J, Evans RW, Moreton K. Williams J, et al. Biochem J. 1978 Aug 1;173(2):533-39. doi: 10.1042/bj1730533. Biochem J. 1978. PMID: 697734 Free PMC article. - Iron-donating properties of transferrin.
Harris DC, Aisen P. Harris DC, et al. Biochemistry. 1975 Jan 28;14(2):262-8. doi: 10.1021/bi00673a011. Biochemistry. 1975. PMID: 1120101 - Functional heterogeneity and pH-dependent dissociation properties of human transferrin.
Princiotto JV, Zapolski EJ. Princiotto JV, et al. Biochim Biophys Acta. 1976 May 28;428(3):766-71. doi: 10.1016/0304-4165(76)90207-5. Biochim Biophys Acta. 1976. PMID: 6057
Cited by
- Properties of a homogeneous C-lobe prepared by introduction of a TEV cleavage site between the lobes of human transferrin.
Steere AN, Roberts SE, Byrne SL, Dennis Chasteen N, Bobst CE, Kaltashov IA, Smith VC, MacGillivray RT, Mason AB. Steere AN, et al. Protein Expr Purif. 2010 Jul;72(1):32-41. doi: 10.1016/j.pep.2010.01.008. Epub 2010 Jan 11. Protein Expr Purif. 2010. PMID: 20064616 Free PMC article. - Interactions of Whey Proteins with Metal Ions.
Rodzik A, Pomastowski P, Sagandykova GN, Buszewski B. Rodzik A, et al. Int J Mol Sci. 2020 Mar 20;21(6):2156. doi: 10.3390/ijms21062156. Int J Mol Sci. 2020. PMID: 32245108 Free PMC article. Review. - Conformational stability of porcine serum transferrin.
Shen ZM, Yang JT, Feng YM, Wu CS. Shen ZM, et al. Protein Sci. 1992 Nov;1(11):1477-84. doi: 10.1002/pro.5560011109. Protein Sci. 1992. PMID: 1303766 Free PMC article. - Iron uptake from rat plasma transferrin by rat reticulocytes.
Huebers H, Huebers E, Csiba E, Finch CA. Huebers H, et al. J Clin Invest. 1978 Nov;62(5):944-51. doi: 10.1172/JCI109223. J Clin Invest. 1978. PMID: 711859 Free PMC article. - The structure and evolution of the murine inhibitor of carbonic anhydrase: a member of the transferrin superfamily.
Eckenroth BE, Mason AB, McDevitt ME, Lambert LA, Everse SJ. Eckenroth BE, et al. Protein Sci. 2010 Sep;19(9):1616-26. doi: 10.1002/pro.439. Protein Sci. 2010. PMID: 20572014 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources