Effects of Trypanocidal Drugs on the Function of Trypanosomes
Abstract
The glycerophosphate oxidase system has been solubilized and partially purified using ubiquinol as an alternate electron donor and octyl glucoside as detergent. Some properties of the solubilized ubiquinol oxidase were investigated. 1) Once the holoenzyme had been in contact with the detergent, 2) glycerol-3-phosphate could no longer be used as substrate, 3) no matter whether the detergent was added during the assay or in the solubilization procedure. However, activity of the oxidase component could then be measured procedure. However, activity of the oxidase component could then be measured with ubiquinol analogs such as CoQ 1, with its isoprenoic side chain, 2,3- dimethoxy-5-methyl-6-nonyl-1,4-benzoquinone (NB) or 2,3-dimethoxy-5-methyl-6- decyl-1, 4-benzoquinone (DB) with their saturated straight chain alkyl groups. NB was preferentially used because it is more stable than CoQ 1, and can be synthesized easily. Keywords: Alpha-glycerophosphate oxidase, Ubiquinol oxidase, Cytochrome b, Maxicircle DNA.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 30, 1983
- Accession Number
- ADA221467
Entities
People
- George C. Hill
Organizations
- Colorado State University