Glutaric acidaemia type II (multiple Acyl‐Coa dehydrogenation deficiency)

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Abstract
The clinical and biochemical phenotype of glutaric acidaemia type II (GAII) has led to the suggestion that the defect in the disorder affects electron transfer from primary FAD-containing dehydrogenases into the respiratory chain. Two proteins are involved in this process, i.e. electron transfer flavoprotein (ETF) and ETF dehydrogenase, an iron-sulphur flavoprotein with a distinctive EPR signal. Reliable catalytic assays for these proteins are not available, but both proteins have been purified and antisera against them prepared in rabbits. SDS-PAG electrophoresis of liver mitochondrial membranes from a GAII infant with congenital anomalies, locating ETF dehydrogenase with specific antiserum, showed no cross-reactive material. EPR of the same membranes showed a marked decrease in the ETF dehydrogenase signal. These results suggest that the defect in GAII in some patients is indeed in electron transport, and specifically in ETF dehydrogenase.

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