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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1993-12-14
|
| pubmed:abstractText |
The kinetic mechanism has been determined for human glutathione S-transferase rho (rho), an isoenzyme related to the human pi (pi) isoenzyme. The kinetic mechanism was investigated by both non-linear regression studies and the analysis of primary and secondary plots, utilizing initial rate and product inhibition data. It was concluded that human isoenzyme rho obeys a random sequential Bi-Bi rapid equilibrium mechanism with the formation of an enzyme-substrate-product (enzyme-CDNB-conjugate) dead-end complex. The values of KCDNB, KGSH and Kconjugate were 0.70 +/- 0.11, 0.12 +/- 0.02 and 0.016 +/- 0.004 mM, respectively. Comparison of the kinetic mechanism and kinetic parameters obtained for glutathione S-transferase isoenzyme rho with other class pi isoenzymes showed similarities at the primary kinetic level.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
10
|
| pubmed:volume |
1203
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
115-20
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1993
|
| pubmed:articleTitle |
Kinetic mechanism of human erythrocyte acidic isoenzyme rho.
|
| pubmed:affiliation |
Department of Medical Biochemistry, University of Cape Town Medical School, Observatory, South Africa.
|
| pubmed:publicationType |
Journal Article,
Comparative Study
|