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3962: 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.*

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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.

Document Language:English
Subject Areas: 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 ...
Funding Part:25-75%
Total budget (Euro):0
Orgprints ID Number:3962
Contact:Nielsen, Head of research unit Jacob Holm
Deposited On:16 November 2004
EPrint Type:Working paper
Published?:Unpublished
Peer Review Status:Not peer-reviewed

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