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Science 12 March 1982:
Vol. 215. no. 4538, pp. 1400 - 1403
DOI: 10.1126/science.7063850
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Articles

Science, Vol 215, Issue 4538, 1400-1403
Copyright © 1982 by American Association for the Advancement of Science

articles

Human liver MAO-A and MAO-B separated by immunoaffinity chromatography with MAO-B-specific monoclonal antibody

RM Denney, RR Fritz, NT Patel, and CW Abell

A monoclonal antibody was used to prepare immunoaffinity columns that efficiently bind monoamine oxidase B activity but not monoamine oxidase A activity from detergent extracts of human liver mitochondria. The only discrete polypeptide component that eluted from affinity columns with potassium thiocyanate migrated in sodium dodecyl sulfate-polyacrylamide gels with an apparent molecular weight of 59,000, as expected for human monoamine oxidase B. These results support the hypothesis that there is an intrinsic structural difference between monoamine oxidase A and B and demonstrate that immunoaffinity chromatography can physically resolve the two enzyme species in liver extracts.


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Characterization of a Highly Conserved FAD-binding Site in Human Monoamine Oxidase B.
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