cDNA-derived amino acid sequence of L-histidine decarboxylase from mouse mastocytoma P-815 cells.
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.
Yamamoto
J
J
Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Yatsunami
K
K
Ohmori
E
E
Sugimoto
Y
Y
Fukui
T
T
Katayama
T
T
Ichikawa
A
A
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D015342:DNA Probes; D006640:Histidine Decarboxylase / Q000235:genetics* / Q000302:isolation & purification; D012515:Mast-Cell Sarcoma / Q000201:enzymology*; D051379:Mice; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid
D015342:DNA Probes; D015345:Oligonucleotide Probes; D006640:Histidine Decarboxylase