| Literature DB >> 44997 |
A J Hillier, R E Jericho, S M Green, G R Jago.
Abstract
The fumarate reductase (NADH) present in cell-free extracts of S. lactis C10 was purified approximately 100-fed by chromatography on DEAE-cellulose in the presence of the non-ionic detergent Teric X-10, and some of the properties of this partially purified enzyme were characterized. Fumarate was able to act as a terminal electron acceptor and decreased the amount of lactate formed and oxygen used during the metabolism of pyruvate by resting cells of S. lactis. Anaerobic growth of S. lactis on glycerol was not observed and fumarate reduction was not coupled with glycerol-3-phosphate oxidation.Entities:
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Year: 1979 PMID: 44997 DOI: 10.1071/bi9790625
Source DB: PubMed Journal: Aust J Biol Sci ISSN: 0004-9417