Changes in LDH Activity in Cryptobranchus Due to Imposed Environmental Stress
Date of Graduation
Spring 1985
Degree
Master of Science in Biology
Department
Biology
Committee Chair
Robert Wilkinson
Abstract
Lactate deydrogenase (LDH), is the enzyme responsible for the conversion of pyruvate to lactic acid. Its activity in the aquatic salamander, Cryptobranchus alleganiensis alleganiensis was studied. Water oxygen saturation was decreased from 100 to 25 to 10% to produce a state of hypoxia, thereby forcing respiration along anaerobic pathways. The effect of increasing temperature (5-25°C) upon the enzyme was also studied. The effects of temperature and oxygen saturation upon hematocrtis were also recorded. Thirteen animals in each of the three temperature groups, at the three oxygen saturations were tested. The results showed that LDH activity increased as oxygen saturation was lowered and that temperatures above 15°C caused a rise in enzyme activity.
Subject Categories
Biology
Copyright
© Norman Reid Brown
Recommended Citation
Brown, Norman Reid, "Changes in LDH Activity in Cryptobranchus Due to Imposed Environmental Stress" (1985). MSU Graduate Theses/Dissertations. 215.
https://bearworks.missouristate.edu/theses/215
Dissertation/Thesis
