[Tryptic peptides of maleylated alpha-chain of histidine decarboxylase from Micrococcus sp. n].

The maleylated alpha-chain of histidine decarboxylase from Micrococcus sp. n., containing 10 arginine residues was hydrolyzed by trypsin, and 9 peptides were isolated from the tryptic hydrolysate. A comparative study of the amino acid sequence in the tryptic peptides of alpha- and beta-chains of histidine decarboxylase allowed to establish the intramolecular homology in the alpha-chain primary structure and homology between the alpha- and beta-chains.