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Modification of rat skeletal muscle hologlyceraldehyde 3-phosphate dehydrogenase by [2,3-14C]butanedione was carried out. The conditions for obtaining preparative amounts of the modified protein and for the maintenance of the modification product stability at various steps of treatment were elaborated. Two radioactive peptides containing modified arginine residues were isolated from the trypsin hydrolysate of the enzyme modified by [2,3-14C] butanedione and oxidizied by performic acid, and their amino acid sequence was established. The data obtained suggest that the essential arginine residue occupies position 134 in the primary structure of the rat muscle enzyme.
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