A novel metalloproteinase originally isolated from brain myelin membranes is present in many tissues.
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.
Department of Neurochemistry, Institute of Neurology, London, U.K.
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Chantry
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Glynn
D000818:Animals; D000911:Antibodies, Monoclonal; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D004229:Dithiothreitol / Q000494:pharmacology; D015151:Immunoblotting; D007163:Immunosorbent Techniques; D008562:Membrane Glycoproteins / Q000032:analysis; D008666:Metalloendopeptidases / Q000032:analysis* / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D008970:Molecular Weight; D004676:Myelin Basic Protein / Q000378:metabolism; D009186:Myelin Sheath / Q000201:enzymology*; D010446:Peptide Fragments / Q000378:metabolism; D014018:Tissue Distribution
D000911:Antibodies, Monoclonal; D008562:Membrane Glycoproteins; D004676:Myelin Basic Protein; D010446:Peptide Fragments; D008666:Metalloendopeptidases; D004229:Dithiothreitol