Changes in LDH Activity in Cryptobranchus Due to Imposed Environmental Stress

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.

Name thesis:degree_name

Master of Science in Biology

Level thesis:degree_level

Masters

Discipline thesis:degree_discipline

Biology

Year

1985

Author dc:creator

• Brown, Norman Reid

Contributors dc:contributor

• Robert Wilkinson

• Biology

Statement dc:rights

• © Norman Reid Brown

Repository record dc:identifier

https://bearworks.missouristate.edu/theses/215

OAI identifier oai:identifier

oai:bearworks.missouristate.edu:theses-1216