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
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antibodies, Monoclonal
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Brain / enzymology*
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Cattle
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Dithiothreitol / pharmacology
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Immunoblotting
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Immunosorbent Techniques
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Membrane Glycoproteins / analysis
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Metalloendopeptidases / analysis*
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Metalloendopeptidases / metabolism
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Mice
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Mice, Inbred BALB C
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Molecular Weight
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Myelin Basic Protein / metabolism
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Myelin Sheath / enzymology*
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Peptide Fragments / metabolism
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Tissue Distribution
Substances
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Antibodies, Monoclonal
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Membrane Glycoproteins
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Myelin Basic Protein
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Peptide Fragments
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Metalloendopeptidases
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Dithiothreitol