Abstract
We studied two patients with 3-methylglutaconic aciduria in order to determine the molecular defect. A new assay for 3-methyl-glutaconyl-coenzyme A (CoA) hydratase has been developed in which the substrate, [5-14C]3-methylglutaconyl-CoA, was synthesized using 3-methylcrotonyl-CoA carboxylase purified from bovine kidney. In this assay the products of the reaction are isolated by reverse-phase high performance liquid chromatography and the rates of conversion from substrate are measured. The Michaelis constant for 3-methylglutaconyl-CoA in normal fibroblast was 6.9 μmol/liter. The mean activity of 3-methyl-glutaconyl-CoA hydratase in control fibroblasts was 495 pmol/min per mg protein. In the two patients the values were 11 and 17 pmol/min per mg protein, or 2-3% of normal.
Original language | English (US) |
---|---|
Pages (from-to) | 1148-1152 |
Number of pages | 5 |
Journal | Journal of Clinical Investigation |
Volume | 77 |
Issue number | 4 |
DOIs | |
State | Published - 1986 |
Externally published | Yes |
ASJC Scopus subject areas
- General Medicine