Abstract
1. 1. Subcellular fractionation of Ascaris muscle was carried out by diffrential centrifugation. A large amount of lipoamide dehydrogenase was found exclusively in microsoaml fraction which had no activities of oxidative decarboxylation of α-ketoacids or glycine. 2. 2. The lipoamide dehydrogenase was easily solubilized and purified to homogeneity from Ascaris muscle microsomes with trypsin, but was not solubilized with 1% Triton X-100. 3. 3. The purified enzyme had a molecular weight of about 97,000 consisting of two subunits whose molecular weight was about 53,000. One molecular of enzyme contained 2 bound molecules of FAD. 4. 4. The amino acid analysis revealed that the amino acid composition of the Ascaris lipoamide dehydrogenase was similar to the lipoamide dehydrogenase from other sources, but tryptophan lacked in it.
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