PURIFICATION OF THE MONOCLONAL HEPARIN ANTIBODY H-1.18

Citation
R. Malsch et al., PURIFICATION OF THE MONOCLONAL HEPARIN ANTIBODY H-1.18, Journal of chromatography, 744(1-2), 1996, pp. 215-221
Citations number
21
Categorie Soggetti
Chemistry Analytical","Biochemical Research Methods
Journal title
Volume
744
Issue
1-2
Year of publication
1996
Pages
215 - 221
Database
ISI
SICI code
Abstract
An antibody of the (immunoglobulin) IgG(1) subclass against heparin wa s purified. Here we report on the purification of the heparin antibody . Ammonium sulfate precipitation was performed and showed a high purit y of the precipitate. In the heparin radioimmunoassay it showed a high heparin binding. Capillary electrophoresis showed that albumin and ot her proteins were separated from the heparin antibody. The purificatio n method allowed a large scale production of the heparin antibody.