cDNA-derived amino acid sequence of L-histidine decarboxylase from mouse mastocytoma P-815 cells

FEBS Lett. 1990 Dec 10;276(1-2):214-8. doi: 10.1016/0014-5793(90)80545-t.

Abstract

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.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • Cloning, Molecular
  • DNA Probes
  • Histidine Decarboxylase / genetics*
  • Histidine Decarboxylase / isolation & purification
  • Mast-Cell Sarcoma / enzymology*
  • Mice
  • Molecular Sequence Data
  • Oligonucleotide Probes
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid

Substances

  • DNA Probes
  • Oligonucleotide Probes
  • Histidine Decarboxylase