Human Liver MAO-A and MAO-B Separated by Immunoaffinity Chromatography with MAO-B-Specific Monoclonal Antibody
- 12 March 1982
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 215 (4538) , 1400-1403
- https://doi.org/10.1126/science.7063850
Abstract
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.This publication has 28 references indexed in Scilit:
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