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

Prozorovskiĭ, V.N.; Grebenshchikova, O.G.; Grebenshcikova, O.G.; Rashkovetskiĭ, L.G.; Prozorovskii, V.N; Grebenshchikova, O.G; Grebenshcikova, O.G; Rashkovetskii, L.G

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

Prozorovskiĭ, V.N.; Grebenshchikova, O.G.; Grebenshcikova, O.G.; Rashkovetskiĭ, L.G.

Biokhimiia 46(2): 269-275

1981

ISSN/ISBN: 0320-9725

PMID: 7248384

Document Number: 174407

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.