Inhibition and Activation of Human Lactate Dehydrogenase by Urea Journal Articles

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.

authors

• Mcqueen, Matthew

status

• published 

publication date

• January 1974

has subject area

• 1101 Medical Biochemistry and Metabolomics (FoR)
• 1103 Clinical Sciences (FoR)
• Butyrates (MeSH)
• Enzyme Activation (MeSH)
• General Clinical Medicine (Science Metrix)
• Humans (MeSH)
• Isoenzymes (MeSH)
• Keto Acids (MeSH)
• L-Lactate Dehydrogenase (MeSH)
• Liver (MeSH)
• Liver Diseases (MeSH)
• Myocardium (MeSH)
• Osmolar Concentration (MeSH)
• Pancreas (MeSH)
• Pyruvates (MeSH)
• Urea (MeSH)

published in

• Annals of Clinical Biochemistry  Journal

keywords

• Butyrates
• Enzyme Activation
• Humans
• Isoenzymes
• Keto Acids
• L-Lactate Dehydrogenase
• Liver
• Liver Diseases
• Myocardium
• Osmolar Concentration
• Pancreas
• Pyruvates
• Urea

Digital Object Identifier (DOI)

• 10.1177/000456327401100131

PubMed ID

• 4413887

start page

• 75

end page

• 80

volume

• 11

issue

• 1-6