Document Type
Thesis
Date of Degree Completion
Fall 1971
Degree Name
Master of Science (MS)
Department
Chemistry
Committee Chair
John E. Meany
Second Committee Member
Robert D. Gaines
Third Committee Member
David G. Lygre
Abstract
The reduction of pyruvate as catalyzed by lactate dehydrogenase has been studied by monitoring the oxidation of DPNH (diphosphopyridine nucleotide) at 340 nm. The kinetic investigation was carried out in phosphate buffer at 25° C. Since pyruvate exists in equilibrium with the enolized and hydrated forms, a kinetic analysis was devised to determine the nature of the true substrate for the enzymatic process. Also, a comparative study was made involving two isozymes of lactate dehydrogenase. The catalytic effectiveness of these isozymes was studied as a function of pH and substrate concentration.
Recommended Citation
Tienhaara, Ronald Floyd, "A Kinetic Study Pertaining to the Enzymatic Reduction of Pyruvate by Lactate Dehydrogenase" (1971). All Master's Theses. 1702.
https://digitalcommons.cwu.edu/etd/1702
Language
English