{"id":{"repo_id":"mo-state","oai_identifier":"oai:bearworks.missouristate.edu:theses-1216"},"canonical_url":"https://search.dev.ndltd.org/etd/mo-state/oai:bearworks.missouristate.edu:theses-1216","repository":{"repo_id":"mo-state","name":"Missouri State University","base_url":"https://bearworks.missouristate.edu/do/oai/"},"display":{"title":"Changes in LDH Activity in Cryptobranchus Due to Imposed Environmental Stress","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.","abstract_html":"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.","abstract_has_math":false,"creators":["Brown, Norman Reid"],"institution":null,"degree_name":"Master of Science in Biology","degree_level":"Masters","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":["Robert Wilkinson"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1985,"date_issued":"1985-05-01T07:00:00Z","date_published":"1985-05-01T07:00:00Z","updated_at":"2026-07-24T03:15:12Z","subjects":["Biology"],"languages":[],"rights":["© Norman Reid Brown"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://bearworks.missouristate.edu/theses/215","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Robert Wilkinson"]},{"key":"dc:creator","label":"Author","values":["Brown, Norman Reid"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science in Biology"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["© Norman Reid Brown"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://bearworks.missouristate.edu/theses/215"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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."]},{"key":"dc:title","label":"Title","values":["Changes in LDH Activity in Cryptobranchus Due to Imposed Environmental Stress"]}]}],"canonical_facts":{"dc:contributor":["Robert Wilkinson"],"dc:creator":["Brown, Norman Reid"],"dc:description.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."],"dc:identifier":["https://bearworks.missouristate.edu/theses/215"],"dc:rights":["© Norman Reid Brown"],"dc:subject":["Biology"],"dc:title":["Changes in LDH Activity in Cryptobranchus Due to Imposed Environmental Stress"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Masters"],"thesis:degree_name":["Master of Science in Biology"]},"updated_at":"2026-07-24T03:15:12Z"}