A novel metalloproteinase originally isolated from brain myelin membranes is present in many tissues

Biochem J. 1990 May 15;268(1):245-8. doi: 10.1042/bj2680245.

Abstract

A monoclonal antibody, CG4, was raised to a novel 60 kDa metalloproteinase purified from a bovine brain myelin glycoprotein fraction. Glycoproteins extracted from both myelin and nine different bovine tissues showed the 60 kDa CG4-immunoreactive band by immunoblotting in amounts that broadly paralleled enzymic activity of this metalloproteinase and varied relatively little among the tissues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal
  • Brain / enzymology*
  • Cattle
  • Dithiothreitol / pharmacology
  • Immunoblotting
  • Immunosorbent Techniques
  • Membrane Glycoproteins / analysis
  • Metalloendopeptidases / analysis*
  • Metalloendopeptidases / metabolism
  • Mice
  • Mice, Inbred BALB C
  • Molecular Weight
  • Myelin Basic Protein / metabolism
  • Myelin Sheath / enzymology*
  • Peptide Fragments / metabolism
  • Tissue Distribution

Substances

  • Antibodies, Monoclonal
  • Membrane Glycoproteins
  • Myelin Basic Protein
  • Peptide Fragments
  • Metalloendopeptidases
  • Dithiothreitol