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Purification of glutathione-binding proteins from bovine milk and identification of glutathione S-transferase

Stagsted, Jan and Nielsen, Jacob H. (2004) Purification of glutathione-binding proteins from bovine milk and identification of glutathione S-transferase. Working paper. [Unpublished]

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Summary

Glutathione is both a ubiquitous and abundant antioxidant in tissues and fluids, and critical as reducing substrate for several enzymes. Particularly, glutathione is utilized by important enzymes, such as glutathione peroxidase (GPx) and glutathione S-transferase (GST). The importance of these glutathione-utilizing enzymes for the oxidative stability of milk is, however, unclear. We have purified glutathione-binding proteins from bovine milk using glutathione-affinity chromatography and report as a novel observation the identification of GST m as a major glutathione-binding protein in bovine milk. GPx was not purified by the glutathione-affinity column.


EPrint Type:Working paper
Subjects: Food systems > Food security, food quality and human health
Research affiliation: Denmark > DARCOF II (2000-2005) > II. 2 (ORMILQ) Production of organic milk of high quality ...
Deposited By: Nielsen, Head of research unit Jacob Holm
ID Code:3962
Deposited On:16 Nov 2004
Last Modified:12 Apr 2010 07:30
Document Language:English
Status:Unpublished
Refereed:Not peer-reviewed

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