Inhibition and Activation of Human Lactate Dehydrogenase by Urea
- 1 January 1974
- journal article
- Published by SAGE Publications in Annals of Clinical Biochemistry: International Journal of Laboratory Medicine
- Vol. 11 (1-6) , 75-80
- https://doi.org/10.1177/000456327401100131
Abstract
The degree of inhibition or activation at 37°C by urea of human lactate dehydrogenase isoenzymes has been established with pyruvate, 2-oxobutyrate, and hydroxypvruvate as substrates. Lactate dehydrogenase activation has been demonstrated in the presence of low concentrations of urea. The protective effect of urea against enzyme inhibition by increased substrate concentrations has also been confirmed. Clinical studies indicate that urea inhibition is a practical and potentially valuable tool in the assessment of LDH isoenzyme patterns at 37°C.Keywords
This publication has 17 references indexed in Scilit:
- An appraisal of routine methods for the determination of the anodal isoenzymes of lactate dehydrogenaseClinica Chimica Acta; International Journal of Clinical Chemistry, 1973
- Optimal Assay of LDH and α-HBD at 37 °CAnnals of Clinical Biochemistry: International Journal of Laboratory Medicine, 1972
- Serumα-Hydroxybutyrate Dehydrogenase Activity: An Improved MethodAmerican Journal of Clinical Pathology, 1971
- UREA INHIBITION OF HUMAN PSEUDOCHOLINESTERASEABritish Journal of Anaesthesia, 1971
- Urea as a selective inhibitor of human tissue alkaline phosphatasesClinica Chimica Acta; International Journal of Clinical Chemistry, 1967
- Clinical applicability of urea-LDH test in various pyruvate concentrationsClinica Chimica Acta; International Journal of Clinical Chemistry, 1967
- Urea and oxalate inhibition of the serum lactate dehydrogenaseJournal of Clinical Pathology, 1965
- Denaturation of Lactic Dehydrogenase Isozymes and its Clinical ApplicationNature, 1965
- Simple Determination of Heart-specific Lactic Dehydrogenase Isoenzyme in SerumNature, 1965
- Structural Characteristics of Dehydrogenases*Biochemistry, 1962