A sensitive and convenient assay procedure for transferrin and its application to the purification of mouse transferrin

E. D. Letendre; B. E. Holbein

doi:10.1139/o81-127

A sensitive and convenient assay procedure for transferrin and its application to the purification of mouse transferrin

E. D. Letendre, B. E. Holbein

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Abstract

A sensitive procedure employing ⁵⁵Fe binding was developed for the assay of transferrin. This procedure took advantage of the pH dependence and reversibility of iron binding by transferrin and was applicable to both human and mouse transferrins. Excess iron, after saturation of the transferrin iron-binding sites with ⁵⁵Fe, supplied as Fe-citrate, was efficiently removed by its binding to Amberlite CG-400 anion-exchange resin. Mouse transferrin was purified from plasma using a combination of ammonium sulphate fractionation and ion-exchange chromatography. Two peaks of pure transferrin were obtained by DEAE-Sepharose chromatography. Mouse transferrin was found to have a molecular weight of 80,000.

Original language	English
Pages (from-to)	906-910
Number of pages	5
Journal	Canadian Journal of Biochemistry
Volume	59
Issue number	11-12
DOIs	https://doi.org/10.1139/o81-127
Publication status	Published - 1981
Externally published	Yes

ASJC Scopus Subject Areas

General Medicine

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Journal Article

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abstract = "A sensitive procedure employing 55Fe binding was developed for the assay of transferrin. This procedure took advantage of the pH dependence and reversibility of iron binding by transferrin and was applicable to both human and mouse transferrins. Excess iron, after saturation of the transferrin iron-binding sites with 55Fe, supplied as Fe-citrate, was efficiently removed by its binding to Amberlite CG-400 anion-exchange resin. Mouse transferrin was purified from plasma using a combination of ammonium sulphate fractionation and ion-exchange chromatography. Two peaks of pure transferrin were obtained by DEAE-Sepharose chromatography. Mouse transferrin was found to have a molecular weight of 80,000.",

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AB - A sensitive procedure employing 55Fe binding was developed for the assay of transferrin. This procedure took advantage of the pH dependence and reversibility of iron binding by transferrin and was applicable to both human and mouse transferrins. Excess iron, after saturation of the transferrin iron-binding sites with 55Fe, supplied as Fe-citrate, was efficiently removed by its binding to Amberlite CG-400 anion-exchange resin. Mouse transferrin was purified from plasma using a combination of ammonium sulphate fractionation and ion-exchange chromatography. Two peaks of pure transferrin were obtained by DEAE-Sepharose chromatography. Mouse transferrin was found to have a molecular weight of 80,000.

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A sensitive and convenient assay procedure for transferrin and its application to the purification of mouse transferrin

Abstract

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