6533b838fe1ef96bd12a4f54
RESEARCH PRODUCT
Messung der gesamtaktivität von glutamat-oxalacetat-transaminase in leberhomogenaten
K.h BässlerW.m Schröckertsubject
chemistry.chemical_classificationChemistryGlutamate dehydrogenaseBiochemistry (medical)Clinical BiochemistryDehydrogenaseGeneral MedicineBiochemistryMolecular biologyTransaminasechemistry.chemical_compoundEnzymeBiochemistryLactate dehydrogenaseLiberationdescription
Abstract A method is described, suitable for routine measurements of the total glutamicoxaloacetic transaminase activity in a large number of liver samples by treatment of homogenates with the detergent Triton X-100. Comparison with other methods and with results of other investigators shows that this method is superior. Neither sonic treatment nor freezing and thawing leads to a complete liberation of the mitochondrial transaminase activity. A number of other enzyme activities can be assayed in Triton-treated homogenates, such as glutamic-pyruvic transaminase, glutamate dehydrogenase, NADP-isocitric dehydrogenase, lactate dehydrogenase, and malate dehy drogenase, β-Hydroxybutyrate dehydrogenase, however, is completely inhibited by Triton X-100.
year | journal | country | edition | language |
---|---|---|---|---|
1971-06-01 | Clinica Chimica Acta |