Purification of the Alpha Glycerophosphate Oxidase from African Trypanosomes
Abstract
Affinity chromatography was employed as the most effective means to purify the glycerophosphate oxidase (GPO). The affinity gel matrix would be coupled with a competitive inhibitor of the dehydrogenase, such as suramin. The dehydrogenase component of th GPO would then bind to the inhibitor. After complete removal of all unattached enzymes, the GPO would be eluted with a buffer containing the substrate alpha-GP. Cyanogen bromide activated Sepharose 4B was coupled to the ligand trypan blue, an analogue of suramin. Trypan blue contains the SO-3 groups and 2-CH3 groups that appear to be essential to 'suramin-like' drug activity against African trypanosomes. Unfortunately, suramin lacks the chemical side-groups to allow it to be attached to the Sepharose 4B affinity gel. Subject terms: Glycerophosphate; Trypanosomes; Sleeping sickness; A-glycerophosphate oxidase; Ubiquinol oxidase; Affinity chromatography; Sepharose 4B.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 02, 1988
- Accession Number
- ADA221492
Entities
People
- George C. Hill
Organizations
- Meharry Medical College