The goal of this project was to study the mechanism of action of gossypol through its (a) binary interaction with native and trypsin digested lactate dehydrogenase-X (LD-X), a sperm-specific isozyme, and (b) its binding in vitro in primary cultures of spermatogenic cells. Mouse LD-X was cleaved with trypsin before and after treatment with gossypol. This was followed by high performance chromatography (HPLC) separation of the LD-X tryptic peptide fragments to observed alterations in separation patterns as indicators of intramolecular disturbance in the enzyme molecule. Definite alterations in peptide fragment peaks were observed in the presence of gossypol and suggest conformational or intramolecular modifications in the enzyme structure attributable to direct binding with gossypol or its degradation products. Whether there are gossypol interactions unique for LD-X was not determined. The binding of 14C-gossypol to cytosolic and membrane fractions of spermatogenic cell suspensions revealed that most of the gossypol was located in the membrane fractions. However, the relative amount of LD-X bound gossypol was greater in the cytosol than the membrane fractions. A model of gossypol binding in spermatogenic cells is proposed.
","abstract_html":"<p>The goal of this project was to study the mechanism of action of gossypol through its (a) binary interaction with native and trypsin digested lactate dehydrogenase-X (LD-X), a sperm-specific isozyme, and (b) its binding in vitro in primary cultures of spermatogenic cells. Mouse LD-X was cleaved with trypsin before and after treatment with gossypol. This was followed by high performance chromatography (HPLC) separation of the LD-X tryptic peptide fragments to observed alterations in separation patterns as indicators of intramolecular disturbance in the enzyme molecule. Definite alterations in peptide fragment peaks were observed in the presence of gossypol and suggest conformational or intramolecular modifications in the enzyme structure attributable to direct binding with gossypol or its degradation products. Whether there are gossypol interactions unique for LD-X was not determined. The binding of <sup>14</sup>C-gossypol to cytosolic and membrane fractions of spermatogenic cell suspensions revealed that most of the gossypol was located in the membrane fractions. However, the relative amount of LD-X bound gossypol was greater in the cytosol than the membrane fractions. A model of gossypol binding in spermatogenic cells is proposed.</p>","abstract_has_math":false,"creators":["Ravenell, Patricia Brown"],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Dissertation","degree_discipline":"Chemistry and Biochemistry","degree_department":null,"school":null,"contributors":["James H. Yuan","Keith Carson","Laura K. Moen","Nancy J. Alexander"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1991,"date_issued":"1991-04-01T08:00:00Z","date_published":"1991-04-01T08:00:00Z","updated_at":"2026-07-24T03:35:23Z","subjects":["Contraception","Gossypol","Lactate dehydrogenase","Biochemistry","Pharmacology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://digitalcommons.odu.edu/biomedicalsciences_etds/127","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["James H. Yuan","Keith Carson","Laura K. Moen","Nancy J. Alexander"]},{"key":"dc:creator","label":"Author","values":["Ravenell, Patricia Brown"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2019-10-16T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry and Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Contraception","Gossypol","Lactate dehydrogenase","Biochemistry","Pharmacology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://digitalcommons.odu.edu/biomedicalsciences_etds/127"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The goal of this project was to study the mechanism of action of gossypol through its (a) binary interaction with native and trypsin digested lactate dehydrogenase-X (LD-X), a sperm-specific isozyme, and (b) its binding in vitro in primary cultures of spermatogenic cells. Mouse LD-X was cleaved with trypsin before and after treatment with gossypol. This was followed by high performance chromatography (HPLC) separation of the LD-X tryptic peptide fragments to observed alterations in separation patterns as indicators of intramolecular disturbance in the enzyme molecule. Definite alterations in peptide fragment peaks were observed in the presence of gossypol and suggest conformational or intramolecular modifications in the enzyme structure attributable to direct binding with gossypol or its degradation products. Whether there are gossypol interactions unique for LD-X was not determined. The binding of 14C-gossypol to cytosolic and membrane fractions of spermatogenic cell suspensions revealed that most of the gossypol was located in the membrane fractions. However, the relative amount of LD-X bound gossypol was greater in the cytosol than the membrane fractions. A model of gossypol binding in spermatogenic cells is proposed.
"]},{"key":"dc:title","label":"Title","values":["A Biochemical Study of Gossypol and Lactate Dehydrogenase X Binary Interactions"]}]}],"canonical_facts":{"dc:contributor":["James H. Yuan","Keith Carson","Laura K. Moen","Nancy J. Alexander"],"dc:creator":["Ravenell, Patricia Brown"],"dc:date.available":["2019-10-16T07:00:00Z"],"dc:description.abstract":["The goal of this project was to study the mechanism of action of gossypol through its (a) binary interaction with native and trypsin digested lactate dehydrogenase-X (LD-X), a sperm-specific isozyme, and (b) its binding in vitro in primary cultures of spermatogenic cells. Mouse LD-X was cleaved with trypsin before and after treatment with gossypol. This was followed by high performance chromatography (HPLC) separation of the LD-X tryptic peptide fragments to observed alterations in separation patterns as indicators of intramolecular disturbance in the enzyme molecule. Definite alterations in peptide fragment peaks were observed in the presence of gossypol and suggest conformational or intramolecular modifications in the enzyme structure attributable to direct binding with gossypol or its degradation products. Whether there are gossypol interactions unique for LD-X was not determined. The binding of 14C-gossypol to cytosolic and membrane fractions of spermatogenic cell suspensions revealed that most of the gossypol was located in the membrane fractions. However, the relative amount of LD-X bound gossypol was greater in the cytosol than the membrane fractions. A model of gossypol binding in spermatogenic cells is proposed.
"],"dc:identifier":["https://digitalcommons.odu.edu/biomedicalsciences_etds/127"],"dc:subject":["Contraception","Gossypol","Lactate dehydrogenase","Biochemistry","Pharmacology"],"dc:title":["A Biochemical Study of Gossypol and Lactate Dehydrogenase X Binary Interactions"],"thesis:degree_discipline":["Chemistry and Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Doctor of Philosophy (PhD)"]},"updated_at":"2026-07-24T03:35:23Z"}