Myoglobin (Mb) and Myoglobin-H (Mb-H) react with glycerophosphocholine (GPC) lipid in the presence of oxygen. This reaction allows the heme group in the protein the chance to induce peroxidation reactions with the lipid. Several aldehyde products of this type of reaction with arachadonic acid have previously been determined, with Mb generating greater quantities of aldehyde products than Mb-H. The focus of this research was to establish the presence of some products from the reactions of Mb and Mb-H with GPC (which contains arachadonic acid) that are more prevalent from Mb-H than Mb, or that only form from the reaction of Mb-H with GPC. A combination of spectrophotometry, TLC, and ion-trapping GC-MS was used to establish the generation of an oxidation product of arachidonic acid metabolism that is generated in larger quantities by the reaction of Mb-H with GPC than by the reaction of Mb with the same lipid.
","abstract_html":"<p>Myoglobin (Mb) and Myoglobin-H (Mb-H) react with glycerophosphocholine (GPC) lipid in the presence of oxygen. This reaction allows the heme group in the protein the chance to induce peroxidation reactions with the lipid. Several aldehyde products of this type of reaction with arachadonic acid have previously been determined, with Mb generating greater quantities of aldehyde products than Mb-H. The focus of this research was to establish the presence of some products from the reactions of Mb and Mb-H with GPC (which contains arachadonic acid) that are more prevalent from Mb-H than Mb, or that only form from the reaction of Mb-H with GPC. A combination of spectrophotometry, TLC, and ion-trapping GC-MS was used to establish the generation of an oxidation product of arachidonic acid metabolism that is generated in larger quantities by the reaction of Mb-H with GPC than by the reaction of Mb with the same lipid.</p>","abstract_has_math":false,"creators":["Lawrence, Kathryn Rae"],"institution":null,"degree_name":"Master of Science (MS)","degree_level":"Open Access Thesis","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Steven Pernecky, Ph.D., Chair","Heather Holmes, Ph.D.","Cory Emal, Ph.D."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2013,"date_issued":"2013-05-01T07:00:00Z","date_published":"2013-05-01T07:00:00Z","updated_at":"2026-07-24T02:16:57Z","subjects":["myoglobin","peroxidation","lipid","Chemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://commons.emich.edu/theses/543","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Steven Pernecky, Ph.D., Chair","Heather Holmes, Ph.D.","Cory Emal, Ph.D."]},{"key":"dc:creator","label":"Author","values":["Lawrence, Kathryn Rae"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2014-04-04T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Open Access Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science (MS)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["myoglobin","peroxidation","lipid","Chemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://commons.emich.edu/theses/543"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Myoglobin (Mb) and Myoglobin-H (Mb-H) react with glycerophosphocholine (GPC) lipid in the presence of oxygen. This reaction allows the heme group in the protein the chance to induce peroxidation reactions with the lipid. Several aldehyde products of this type of reaction with arachadonic acid have previously been determined, with Mb generating greater quantities of aldehyde products than Mb-H. The focus of this research was to establish the presence of some products from the reactions of Mb and Mb-H with GPC (which contains arachadonic acid) that are more prevalent from Mb-H than Mb, or that only form from the reaction of Mb-H with GPC. A combination of spectrophotometry, TLC, and ion-trapping GC-MS was used to establish the generation of an oxidation product of arachidonic acid metabolism that is generated in larger quantities by the reaction of Mb-H with GPC than by the reaction of Mb with the same lipid.
"]},{"key":"dc:title","label":"Title","values":["Arachidonate oxidation metabolite profiles for myoglobin and a structurally altered form of myoglobin produced in muscle disease or trauma"]}]}],"canonical_facts":{"dc:contributor":["Steven Pernecky, Ph.D., Chair","Heather Holmes, Ph.D.","Cory Emal, Ph.D."],"dc:creator":["Lawrence, Kathryn Rae"],"dc:date.available":["2014-04-04T07:00:00Z"],"dc:description.abstract":["Myoglobin (Mb) and Myoglobin-H (Mb-H) react with glycerophosphocholine (GPC) lipid in the presence of oxygen. This reaction allows the heme group in the protein the chance to induce peroxidation reactions with the lipid. Several aldehyde products of this type of reaction with arachadonic acid have previously been determined, with Mb generating greater quantities of aldehyde products than Mb-H. The focus of this research was to establish the presence of some products from the reactions of Mb and Mb-H with GPC (which contains arachadonic acid) that are more prevalent from Mb-H than Mb, or that only form from the reaction of Mb-H with GPC. A combination of spectrophotometry, TLC, and ion-trapping GC-MS was used to establish the generation of an oxidation product of arachidonic acid metabolism that is generated in larger quantities by the reaction of Mb-H with GPC than by the reaction of Mb with the same lipid.
"],"dc:identifier":["https://commons.emich.edu/theses/543"],"dc:subject":["myoglobin","peroxidation","lipid","Chemistry"],"dc:title":["Arachidonate oxidation metabolite profiles for myoglobin and a structurally altered form of myoglobin produced in muscle disease or trauma"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Open Access Thesis"],"thesis:degree_name":["Master of Science (MS)"]},"updated_at":"2026-07-24T02:16:57Z"}