-transparent.png){kind=logo}
An improved method for the assay of human platelet pyruvate dehydrogenase is described. By generating the substrate [1-14C]pyruvate in situ from [1-14C]lactate plus L-lactate dehydrogenase, the rate of spontaneous decarboxylation is dramatically reduced, allowing far greater sensitivity in the assay of low activities of pyruvate dehydrogenase. In addition, no special precautions are required for the storage and use of [1-14C]lactate, in contrast to those for [1-14C]pyruvate. These factors allow a 5-10-fold increase in sensitivity compared with current methods. The pyruvate dehydrogenase activity of normal subjects as determined by the [1-14C]lactate system was 215 +/- 55 pmol . min-1 . mg-1 protein (n = 18). The advantages of this assay system are discussed.
P J Schofield, and
L R Griffiths, and
S H Rogers, and
G Wise
September 1979,
Analytical biochemistry,
P J Schofield, and
L R Griffiths, and
S H Rogers, and
G Wise
June 1992,
The Biochemical journal,
P J Schofield, and
L R Griffiths, and
S H Rogers, and
G Wise
July 1991,
The Biochemical journal,
P J Schofield, and
L R Griffiths, and
S H Rogers, and
G Wise
September 1995,
Clinica chimica acta; international journal of clinical chemistry,
P J Schofield, and
L R Griffiths, and
S H Rogers, and
G Wise
August 1993,
Analytical biochemistry,
P J Schofield, and
L R Griffiths, and
S H Rogers, and
G Wise
November 1973,
Analytical biochemistry,
P J Schofield, and
L R Griffiths, and
S H Rogers, and
G Wise
July 1973,
Analytical biochemistry,
P J Schofield, and
L R Griffiths, and
S H Rogers, and
G Wise
November 1992,
Biochimica et biophysica acta,
P J Schofield, and
L R Griffiths, and
S H Rogers, and
G Wise
April 1974,
The Biochemical journal,
P J Schofield, and
L R Griffiths, and
S H Rogers, and
G Wise
September 1967,
Endocrinology,
