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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1976-4-9
|
| pubmed:abstractText |
In cell free extract from Neisseria meningitidis an enzyme has been found which catalyses the oxidation of L-malate to oxaloacetate in the absence of pyridine nucleotides, using ferricyanide as electron acceptor. The enzyme was found to be particle-bound, as determined by sucrose gradient centrifugation. Activity corresponding to this enzyme was demonstrated in extracts from all strains tested of selected Neisseria species. In contrast to the large differences in NAD-linked malate dehydrogenase activity among the species, the interspecies variation of the pyridine nucleotide independent oxidation of malate was not sufficiently distinct to be useful for classification purposes.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0105-0656
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
84
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
17-21
|
| pubmed:dateRevised |
2009-6-4
|
| pubmed:meshHeading |
pubmed-meshheading:814782-Cell-Free System,
pubmed-meshheading:814782-Citric Acid Cycle,
pubmed-meshheading:814782-Malate Dehydrogenase,
pubmed-meshheading:814782-Malates,
pubmed-meshheading:814782-Neisseria,
pubmed-meshheading:814782-Neisseria gonorrhoeae,
pubmed-meshheading:814782-Neisseria meningitidis,
pubmed-meshheading:814782-Oxaloacetates,
pubmed-meshheading:814782-Oxidation-Reduction,
pubmed-meshheading:814782-Pyridines
|
| pubmed:year |
1976
|
| pubmed:articleTitle |
Pyridine nucleotide independent oxidation of L-malate in genus Neisseria.
|
| pubmed:publicationType |
Journal Article
|