Abstract
Hydrogen carrier protein (H-protein), a component of the glycine cleavage system, has been purified to homogeneity from chicken liver mitochondria. The molecular weight and the partial specific volume determined by two different methods were 14,500 and 0.724 ml/g, respectively. The protein has an isoelectric point of 4.0. Amino acid analysis revealed 131 residues, about one-third of which are acidic residues. Evidence is presented indicating that the protein contains one lipoic acid moiety per molecule. In the decarboxylation of glycine the disulfide of the lipoyl moiety is cleaved and one of the resultant sulf-hydryl groups receives an intermediate derived from glycine.
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