cDNA cloning and sequence determination of rat membrane-associated phospholipase A2

Biochem Biophys Res Commun. 1989 Aug 15;162(3):1030-6. doi: 10.1016/0006-291x(89)90777-8.

Abstract

Based on the partial amino acid sequences of membrane-associated phospholipase A2 (PLA2M), belonging to group II, purified from rat spleen, the cDNA encoding PLA2M was cloned by a new cloning strategy utilizing enzymatic cDNA amplification. At the N-terminus of the coded 146 residues, which were deduced from the cDNA sequence, the putative signal peptide was found despite the tight adherence of this enzyme to the membrane. The sequence of rat PLA2M exhibits 75% homology with that of human group II PLA2 in the protein-coding region. The result of RNA blot analysis showed that rat ileal mucosa contains the largest amount of the PLA2 transcript among the tissues examined.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Northern
  • Cell Membrane / enzymology
  • Cloning, Molecular
  • DNA / genetics
  • Gene Amplification
  • Molecular Sequence Data
  • Oligonucleotide Probes
  • Phospholipases / genetics*
  • Phospholipases A / genetics*
  • Phospholipases A2
  • Rats
  • Spleen / enzymology

Substances

  • Oligonucleotide Probes
  • DNA
  • Phospholipases
  • Phospholipases A
  • Phospholipases A2

Associated data

  • GENBANK/M25148