Monoclonal Antibodies to Human Lysyl Oxidase
Document Type
Article
Date of Original Version
1-1-1986
Abstract
Hybridoma antibodies against human lysyl oxidase were produced by fusing Sp. 2.0-Ag 14 myeloma cells with spleen cells from mice hyperimmunized with lysyl oxidase isolated from umbilical cords. Hybridomas positive by enzyme-linked immunosorbent assay (ELISA) for human lysyl oxidase were cloned by the dilution method. Eight hybridomas producing antibodies were isolated, three of which also recognized purified bovine aortic lysyl oxidase in an ELISA. One of these antibodies, monoclonal antibody I, was purified and attached to Sepharose CL-4B. The immobilized antibody was effective in binding an enzymatically active 30,000 dalton species. Immunoblot analysis of four of these antibodies showed reactivity against dic 30,000 dalton catalytically active enzyme and the 24,000 dalton fragment of lysyl oxidase. These monoclonal antibodies should be useful tools for studying the localization and biosynthesis of lysyl oxidase. © 1986, Gustav Fischer Verlag · Stuttgart · New York. All rights reserved.
Publication Title, e.g., Journal
Topics in Catalysis
Volume
6
Issue
2
Citation/Publisher Attribution
Burbelo, Peter D., Monckeberg, and Clinton O. Chichester. "Monoclonal Antibodies to Human Lysyl Oxidase." Topics in Catalysis 6, 2 (1986): 153-162. doi: 10.1016/S0174-173X(86)80022-X.