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Coimmobilization of Lactate Dehydrogenase and Low-Molecular-Weight Thiols on Sepharose

Coimmobilization of Lactate Dehydrogenase and Low-Molecular-Weight Thiols on Sepharose Lactate dehydrogenase (EC 1.1.1.27) and dithiothreitol (DTT) were coimmobilized on Sepharose activated with cyanogen bromide. It was demonstrated that the addition of 10 mM DTT (but not 2-mercaptoethanol) during immobilization increased the enzyme specific activity 1.5–5-fold depending on the initial extent of Sepharose activation by cyanogen bromide. The total activity increased two- to threefold. The lactate dehydrogenase preparations were rich in matrix-immobilized sulfhydryl groups (1.8–13.0 nmol per ml gel). The presence of DTT increased the stability of immobilized lactate dehydrogenase. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Coimmobilization of Lactate Dehydrogenase and Low-Molecular-Weight Thiols on Sepharose

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References (10)

Publisher
Springer Journals
Copyright
Copyright © 2001 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Medical Microbiology; Biochemistry, general; Microbiology
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1023/A:1002831932006
Publisher site
See Article on Publisher Site

Abstract

Lactate dehydrogenase (EC 1.1.1.27) and dithiothreitol (DTT) were coimmobilized on Sepharose activated with cyanogen bromide. It was demonstrated that the addition of 10 mM DTT (but not 2-mercaptoethanol) during immobilization increased the enzyme specific activity 1.5–5-fold depending on the initial extent of Sepharose activation by cyanogen bromide. The total activity increased two- to threefold. The lactate dehydrogenase preparations were rich in matrix-immobilized sulfhydryl groups (1.8–13.0 nmol per ml gel). The presence of DTT increased the stability of immobilized lactate dehydrogenase.

Journal

Applied Biochemistry and Microbiology – Springer Journals

Published: Oct 19, 2004

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