Purification of transferrin from Cohn supernatant I using ion-exchange chromatography

Karl B. McCann; Ben Hughes; John Wu; Joseph Bertolini; Peter T. Gomme

doi:10.1042/BA20050065

Purification of transferrin from Cohn supernatant I using ion-exchange chromatography

Karl B. McCann, Ben Hughes, John Wu, Joseph Bertolini, Peter T. Gomme

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

Abstract

The present paper describes an anion-exchange chromatography method to separate iron-free apo-Tf (apo-transferrin) from albumin and IgG in Cohn supernatant I. The method uses DEAE-fast flow Sepharose chromatography along with optimized protein concentration (5%, w/v) and column operation conditions (40 g/l, conductivity < 1.0 mS/cm) to resolve apo-Tf from IgG and albumin. The single step purifies apo-Tf to > 90% and provides an efficient means to obtain commercial quantities of the protein.

Original language	English
Pages (from-to)	211-217
Number of pages	7
Journal	Biotechnology and Applied Biochemistry
Volume	42
Issue number	3
DOIs	https://doi.org/10.1042/BA20050065
Publication status	Published - Dec 1 2005
Externally published	Yes

Keywords

Cohn supernatant I
Human serum albumin (HSA)
Ion-exchange chromatography
Iron transport
Plasma
Transferrin

ASJC Scopus subject areas

Biotechnology
Bioengineering
Molecular Medicine
Biomedical Engineering
Applied Microbiology and Biotechnology
Drug Discovery
Process Chemistry and Technology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1042/BA20050065

Cite this

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abstract = "The present paper describes an anion-exchange chromatography method to separate iron-free apo-Tf (apo-transferrin) from albumin and IgG in Cohn supernatant I. The method uses DEAE-fast flow Sepharose chromatography along with optimized protein concentration (5%, w/v) and column operation conditions (40 g/l, conductivity < 1.0 mS/cm) to resolve apo-Tf from IgG and albumin. The single step purifies apo-Tf to > 90% and provides an efficient means to obtain commercial quantities of the protein.",

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AU - McCann, Karl B.

AU - Hughes, Ben

AU - Wu, John

AU - Bertolini, Joseph

AU - Gomme, Peter T.

PY - 2005/12/1

Y1 - 2005/12/1

N2 - The present paper describes an anion-exchange chromatography method to separate iron-free apo-Tf (apo-transferrin) from albumin and IgG in Cohn supernatant I. The method uses DEAE-fast flow Sepharose chromatography along with optimized protein concentration (5%, w/v) and column operation conditions (40 g/l, conductivity < 1.0 mS/cm) to resolve apo-Tf from IgG and albumin. The single step purifies apo-Tf to > 90% and provides an efficient means to obtain commercial quantities of the protein.

AB - The present paper describes an anion-exchange chromatography method to separate iron-free apo-Tf (apo-transferrin) from albumin and IgG in Cohn supernatant I. The method uses DEAE-fast flow Sepharose chromatography along with optimized protein concentration (5%, w/v) and column operation conditions (40 g/l, conductivity < 1.0 mS/cm) to resolve apo-Tf from IgG and albumin. The single step purifies apo-Tf to > 90% and provides an efficient means to obtain commercial quantities of the protein.

KW - Cohn supernatant I

KW - Human serum albumin (HSA)

KW - Ion-exchange chromatography

KW - Iron transport

KW - Plasma

KW - Transferrin

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Purification of transferrin from Cohn supernatant I using ion-exchange chromatography

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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