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cDNA‐derived amino acid sequence of L‐histidine decarboxylase from mouse mastocytoma P‐815 cells
Author(s) -
Yamamoto Jun,
Yatsunami Kimio,
Ohmori Eiji,
Sugimoto Yukihiko,
Fukui Tetsuya,
Katayama Toyoko,
Ichikawa Atsushi
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80545-t
Subject(s) - histidine decarboxylase , mastocytoma , complementary dna , microbiology and biotechnology , nucleic acid sequence , peptide sequence , protein primary structure , histidine , biology , cdna library , biochemistry , amino acid , homology (biology) , chemistry , gene , in vitro
The primary structure of L‐histidine decarboxylase (HDC: L‐histidine carboxy‐lyase, EC 4.1.1.22) from mouse mastocytoma P‐815 cells has been determined by parallel analysis of the amino acid sequence of the protein and the nucleotide sequence of the corresponding cDNA. HDC contains 662 amino acid residues with a molecular mass of 74017, which is larger by about 21 000 Da than that of the previously purified HDC subunit (53 kDa), suggesting that HDC might be posttranslationally processed. The HDC cDNA hybridized to a 2.7 kilobase mRNA of mastocytoma cells. Homology was found between the sequences of mouse mastocytoma HDC and fetal rat liver HDC.