Feb 1, 1976

Lipoamide dehydrogenase in serum: a preliminary report

Clinical Chemistry
J W PelleyF F Hall

Abstract

Lipoamide dehydrogenase was identified in serum and the optimal conditions for its assay at 30 degrees C were defined. The pH optimum in tris(hydroxymethyl)aminomethane buffer is 7.8, and activity is inhibited if buffer concentration exceeds 100 mmol/liter. Saturating concentrations of the substrates NAD+ and lipoamide are 3 mmol/liter and 5 mmol/liter, respectively. Activity is decreased eightfold when lipoic acid is substituted for lipoamide. Activity is linearly related to enzyme concentration up to limiting absorbance change of 0.300 at 340 nm, and both within-day and day-to-day precision are satisfactory. Data suggest a normal range (2 SD) of 3-19 kU/liter. The highest value measured in serum was 473 kU/liter. A correlation with direct bilirubin concentrations (r equals 0.435, P less than 0.01) was found.

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Mentioned in this Paper

Bilirubin, Direct Measurement
Tromethamine
Bilirubin, (4E,15E)-Isomer
NADH
Lipoamide
Ampholytes
Dihydrolipoamide Dehydrogenase
Thioctic Acid
DLD gene
Direct reacting bilirubin

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