Source:http://linkedlifedata.com/resource/pubmed/id/17029890
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-3
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| pubmed:dateCreated |
2006-10-10
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| pubmed:abstractText |
The pH dependence of squash-leaf nitrate reductase has been studied. It has been found that high- and low-activity forms of purified nitrate reductase (both forms dephosphorylated) have different optimum pH values. A high-activity form has always a higher pH optimum compared with a low-activity form. Model computations show that the decrease in activity and the corresponding change of the pH optimum is apparently due to a conformation-dependent increase of proton dissociation of the enzyme. As previously shown, this behavior is also observed in leaf extracts during the conversion (and probably phosphorylation of nitrate reductase) from a high-active form to a low-active form when plants are transferred from light to darkness.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0301-4622
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
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| pubmed:volume |
67
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
59-64
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| pubmed:year |
1997
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| pubmed:articleTitle |
Evidence for increased proton dissociation in low-activity forms of dephosphorylated squash-leaf nitrate reductase.
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| pubmed:affiliation |
Stavanger College, School of Technology and Science, P.O. Box 2557 Ullandhaug, 4004 Stavanger, Rogaland, Norway.
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| pubmed:publicationType |
Journal Article
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