Date of Publication
2006
Document Type
Master's Thesis
Degree Name
Master of Science in Chemistry
Subject Categories
Chemistry
College
College of Science
Department/Unit
Chemistry
Thesis Adviser
Nancy Lazaro Llanos
Defense Panel Chair
Marissa G. Noel
Defense Panel Member
Julita C. Robles
Myrna P. Tepora
Abstract/Summary
Lactate dehydrogenase or LDH (EC. 1.1.1.27), an anaerobic glycolysis enzyme present in all vertebrates, was isolated from the skeletal and heart muscle tissues of domestic pig, Sus scrofa cristatus. The crude sample was purified using a series of techniques including centrifugation, dialysis, and salt precipitation. Further purification process in the form of gel filtration chromatography was carried out in the last stage to maximize the degree of purity of the enzyme. At each stage of purification, specific enzyme and protein concentration assays, employing the principles of ultraviolet (UV) absorption spectroscopy, were applied to each fraction collected in order to determine the degree of purification thus attained using the specified technique. The last fraction obtained, which was the enzyme fraction with the highest level of purity, was finally subjected to a kinetic study for the determination of parameters like Michaelis constant, maximum velocity, catalytic constant, and catalytic efficiency.
Abstract Format
html
Language
English
Format
Electronic
Accession Number
CDTG004357
Shelf Location
Archives, The Learning Commons, 12F Henry Sy Sr. Hall
Physical Description
Xi, 99 leaves ; 28 cm.
Keywords
Lactate Dehydrogenase; Centrifugation
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Recommended Citation
Pangilinan, C. M. (2006). Isolation, purification, and kinetic study of lactate dehydrogenase from porcine skeletal and cardiac muscle tissues. Retrieved from https://animorepository.dlsu.edu.ph/etd_masteral/3535
