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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1980-5-30
|
| pubmed:abstractText |
Bovine lens aldose reductase, an enzyme important in sugar cataract formation, has been purified using a new procedure, and its optimum conditions of assay defined in both lens homogenates and purified preparations. Preliminary kinetic analysis shows that the degree of the rate equation is of a low order, and may be Michaelian under the standard conditions used.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0009-9120
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
12
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
281-3
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1979
|
| pubmed:articleTitle |
Kinetic behaviour under defined assay conditions for bovine lens aldose reductase.
|
| pubmed:publicationType |
Journal Article
|