[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.
D000595:Amino Acid Sequence; D002262:Carboxy-Lyases; D006640:Histidine Decarboxylase; D046911:Macromolecular Substances; D008298:Maleates; D008837:Micrococcus / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D046911:Macromolecular Substances; D008298:Maleates; D010446:Peptide Fragments; D014357:Trypsin; D002262:Carboxy-Lyases; D006640:Histidine Decarboxylase
Tripticheskie peptidy maleilirovannoĭ al'fa-tsepi gistidindekarboksilazy Micrococcus sp. n.