An Initial Reaction Rate Assay for "Glycerate Dehydrogenase" Journal Articles

abstract

• Abstract Concentrations of substrate, coenzyme, and hydrogen ion, optimal for the reduction of hydroxypyruvate at 37°C by normal and pathological human sera are described. We confirmed, by using the supernatant fluid from homogenized human heart and liver tissue, that the faster-moving isoenzymes have a greater affinity for substrate and coenzyme than the slowermoving isoenzymes, which require higher concentrations for saturation. LDHx, present in human seminal plasma, appears to have the lowest Michaelis constant for hydroxypyruvate. Glycerate dehydrogenase was found to be stable if the standard assay temperature was increased from 25° to 37°C.

authors

• Mcqueen, Matthew
• King, J

status

• published 

publication date

• November 1, 1971

has subject area

• 1004 Medical Biotechnology (FoR)
• 1101 Medical Biochemistry and Metabolomics (FoR)
• 1103 Clinical Sciences (FoR)
• Alcohol Oxidoreductases (MeSH)
• Blood Protein Electrophoresis (MeSH)
• Drug Stability (MeSH)
• General Clinical Medicine (Science Metrix)
• Glyceric Acids (MeSH)
• Hot Temperature (MeSH)
• Humans (MeSH)
• Hydrogen-Ion Concentration (MeSH)
• Hydroxybutyrates (MeSH)
• In Vitro Techniques (MeSH)
• Isoenzymes (MeSH)
• Kinetics (MeSH)
• L-Lactate Dehydrogenase (MeSH)
• Lactates (MeSH)
• Liver (MeSH)
• Myocardium (MeSH)
• Pyruvates (MeSH)
• Semen (MeSH)

published in

• Clinical Chemistry  Journal

keywords

• Alcohol Oxidoreductases
• Blood Protein Electrophoresis
• Drug Stability
• Glyceric Acids
• Hot Temperature
• Humans
• Hydrogen-Ion Concentration
• Hydroxybutyrates
• In Vitro Techniques
• Isoenzymes
• Kinetics
• L-Lactate Dehydrogenase
• Lactates
• Liver
• Myocardium
• Pyruvates
• Semen

Digital Object Identifier (DOI)

• 10.1093/clinchem/17.11.1089

PubMed ID

• 5127365

start page

• 1089

end page

• 1092

volume

• 17

issue

• 11