Partial purification and characterisation of a 31 kDalton putative enkephalin precursor from guinea pig striatum

Neuropeptides. 1985 Feb;5(4-6):505-8. doi: 10.1016/0143-4179(85)90065-4.

Abstract

The presence of several putative precursors for Met-enkephalin (ME) and Leu-enkephalin (LE) has been demonstrated in guinea pig striatal extracts. The major high molecular weight (Mr) species (31000) contained 9% of the total ME-immunoreactivity (IR) after digest. This species has been partially purified and characterized using sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and nitrocellulose blotting techniques as well as highly specific radioimmunoassay (RIA) for ME, LE and ME-Arg6-Phe7.

MeSH terms

  • Animals
  • Carboxypeptidase B
  • Carboxypeptidases
  • Catalysis
  • Corpus Striatum / analysis*
  • Electrophoresis, Polyacrylamide Gel
  • Endopeptidases
  • Enkephalins / isolation & purification*
  • Guinea Pigs
  • Male
  • Metalloendopeptidases*
  • Protein Precursors / isolation & purification*
  • Trypsin

Substances

  • Enkephalins
  • Protein Precursors
  • Carboxypeptidases
  • Endopeptidases
  • Carboxypeptidase B
  • Trypsin
  • Metalloendopeptidases
  • auR protein, Staphylococcus aureus