Immunological characterization of bovine lysyl oxidase
Document Type
Article
Date of Original Version
1-1-1985
Abstract
1. 1. Antibodies to homogeneously purified bovine aortic lysyl oxidase were prepared in chickens. 2. 2. The chicken anti-lysyl oxidase antiserum effectively inhibited bovine aortic lysyl oxidase activity. Non-immune antiserum from chickens, goats and humans was found to enhance bovine aortic lysyl oxidase activity, while non-immune rabbit serum inhibited enzyme activity. 3. 3. A competitive ELISA was developed to monitor immunoreactive lysyl oxidase during purification. 4. 4. Chromatography of bovine lysyl oxidase on Sephacryl S-200, the final step in purification, revealed two peaks of immunoreactive lysyl oxidase. The large molecular weight peak appears to contain inactive multimeric forms of the enzyme. © 1985.
Publication Title, e.g., Journal
Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume
81
Issue
4
Citation/Publisher Attribution
Burbelo, P. D., M. Kagan, and C. O. Chichester. "Immunological characterization of bovine lysyl oxidase." Comparative Biochemistry and Physiology -- Part B: Biochemistry and 81, 4 (1985): 845-849. doi: 10.1016/0305-0491(85)90077-X.