Journal article
Pyridine Nucleotide-Linked Lactate Dehydrogenase of Tetrahymena: Evidence for D- and L-Enzymes in the Mitochondria
JOURNAL OF EUKARYOTIC MICROBIOLOGY, v 68(3), e12851
May 2021
PMID: 33749960
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
An NAD-linked lactate dehydrogenase (LDH) in a crude mitochondrial fraction obtained from Tetrahymena homogenates was previously reported by this laboratory. This fraction contains the NADH and succinate oxidase system as well as the mitochondrial cytochromes and carries out oxidative phosphorylation. The preparation catalyzes the oxidation of D- and L-lactate linked only to certain analogs of NAD; it has not been possible to demonstrate NAD-dependent D- or L-lactate oxidation nor is there any evidence that either of these enzymes is a flavoprotein as indicated by their inability to reduce directly certain artificial electron acceptors. A lactate racemase is not present.
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Details
- Title
- Pyridine Nucleotide-Linked Lactate Dehydrogenase of Tetrahymena: Evidence for D- and L-Enzymes in the Mitochondria
- Publication Details
- JOURNAL OF EUKARYOTIC MICROBIOLOGY, v 68(3), e12851
- Publisher
- WILEY; HOBOKEN
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Drexel University
- Web of Science ID
- WOS:000640184000001
- Scopus ID
- 2-s2.0-85104337072
- Other Identifier
- 991021860758404721
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- Web of Science research areas
- Microbiology