TY - JOUR
AU - Hall, F, F
AB - 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. This content is only available as a PDF. © 1976 The American Association for Clinical Chemistry, Inc. This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)
TI - Lipoamide dehydrogenase in serum: a preliminary report.
JF - Clinical Chemistry
DO - 10.1093/clinchem/22.2.275
DA - 1976-02-01
UR - https://www.deepdyve.com/lp/oxford-university-press/lipoamide-dehydrogenase-in-serum-a-preliminary-report-0QuvdQAiZB
SP - 275
EP - 277
VL - 22
IS - 2
DP - DeepDyve
ER -