Abstract
1. 1. Lactate dehydrogenase (LDH) of the culture from Trypanosoma conorhini has an activity of 158 units/min per mg protein and is composed of five isozymes. This LDH had abnormal Michaelis-Menten kinetics and is denatured by 2 M urea. 2. 2. LDH activities of the kinetoplastic and dyskinetoplastic bloodstream forms of T. equiperdum are 23 and 33 units/min per mg protein, respectively. LDHs of both forms are composed of two isozymes. 3. 3. The malate dehydrogenase (MDH) activity of T. conorhini is 7337 units/min per mg protein. The MDH is composed of two isozymes when NAD is used and three isozymes when NADP is used as the cofactor. The anodal isozyme was the mitochondrial MDH and the soluble fraction contained both MDH isozymes. 4. 4. The MDH activity of the kinetoplastic and dyskinetoplastic forms of T. equiperdum are, respectively, 355 and 298 units/min per mg protein. The MDH of both forms was composed of three closely spaced cathodal isozymes. 5. 5. LDH increased in activity as the T. conorhini cultures aged. MDH increased and LDH decreased in cultures with a larger surface to volume ratio than the cultures normally used.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
