{"id":{"repo_id":"vt","oai_identifier":"oai:vtechworks.lib.vt.edu:10919/53186"},"canonical_url":"https://search.dev.ndltd.org/etd/vt/oai:vtechworks.lib.vt.edu:10919/53186","repository":{"repo_id":"vt","name":"Virginia Tech","base_url":"https://vtechworks.lib.vt.edu/oai/request"},"display":{"title":"The relationship between two forms of glycogen phosphorylase in Dictyostelium discoideum","abstract":"The cellular slime mold, Dictyortelium dixcoideum, provides an ideal model system to study eukaryotic cell differentiation. In D. discoideum glycogen degradation provides precursors for the synthesis of developmentally regulated structural end products. The enzyme responsible for glycogen degradation, glycogen phosphorylase, exists in active and inactive forms. The activity of the ’a' form (the active form) is independent of 5′adenosine monophosphate (5′AMP) while the activity of the ’b' form (the inactive form) is 5′AMP dependent, The two forms are developmentally regulated. Polyclortal antibodies raised to the purified forms of this enzyme show low cross reactivity. The anti-’a' antiserum reacts with a 104 kd protein that is associated with phosphorylase ’a' activity; the anti-’b' antiserum reacts with a 92 kd protein that is associated with phosphorylase ’b' activity and cross reacts weakly with the 104 kd protein. Cyclic AMP perturbation of intact cells caused induction of both phosphorylase ’a' activity and the appearance of the 104 kd protein. lmmunotitration data suggest that the ’a’ form accumulates due to de novo protein synthesis, although this result must be interpreted with caution. In vitro translation experiments indicate that separate mRNA species exist for the two forms of phosphorylase. The mRNA for the 'b’ form is present throughout development while that of the ’a' form appears late in development.","abstract_html":"The cellular slime mold, Dictyortelium dixcoideum, provides an ideal model system to study eukaryotic cell differentiation. In D. discoideum glycogen degradation provides precursors for the synthesis of developmentally regulated structural end products. The enzyme responsible for glycogen degradation, glycogen phosphorylase, exists in active and inactive forms. The activity of the ’a' form (the active form) is independent of 5′adenosine monophosphate (5′AMP) while the activity of the ’b' form (the inactive form) is 5′AMP dependent, The two forms are developmentally regulated. Polyclortal antibodies raised to the purified forms of this enzyme show low cross reactivity. The anti-’a' antiserum reacts with a 104 kd protein that is associated with phosphorylase ’a' activity; the anti-’b' antiserum reacts with a 92 kd protein that is associated with phosphorylase ’b' activity and cross reacts weakly with the 104 kd protein. Cyclic AMP perturbation of intact cells caused induction of both phosphorylase ’a' activity and the appearance of the 104 kd protein. lmmunotitration data suggest that the ’a’ form accumulates due to de novo protein synthesis, although this result must be interpreted with caution. In vitro translation experiments indicate that separate mRNA species exist for the two forms of phosphorylase. The mRNA for the 'b’ form is present throughout development while that of the ’a' form appears late in development.","abstract_has_math":false,"creators":["Sucic, Joseph F."],"institution":"Virginia Polytechnic Institute and State University","degree_name":"Master of Science","degree_level":"masters","degree_discipline":"Biology","degree_department":"Biology","school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1988,"date_issued":"1988","date_published":"1988","updated_at":"2026-07-22T22:19:37Z","subjects":[],"languages":["en_US"],"rights":["In Copyright"],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10919/53186","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.department","label":"Department","values":["Biology"]},{"key":"dc:creator","label":"Author","values":["Sucic, Joseph F."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2015-06-23T19:09:25Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2015-06-23T19:09:25Z"]},{"key":"dc:date.issued","label":"Date","values":["1988"]},{"key":"dc:publisher","label":"Institution","values":["Virginia Polytechnic Institute and State University"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.dcmitype","label":"Dc Type Dcmitype","values":["Text"]},{"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"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Virginia Polytechnic Institute and State University"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en_US"]},{"key":"dc:rights","label":"Dc Rights","values":["In Copyright"]},{"key":"dc:rights.uri","label":"Rights URI","values":["http://rightsstatements.org/vocab/InC/1.0/"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10919/53186"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The cellular slime mold, Dictyortelium dixcoideum, provides an ideal model system to study eukaryotic cell differentiation. In D. discoideum glycogen degradation provides precursors for the synthesis of developmentally regulated structural end products. The enzyme responsible for glycogen degradation, glycogen phosphorylase, exists in active and inactive forms. The activity of the ’a' form (the active form) is independent of 5′adenosine monophosphate (5′AMP) while the activity of the ’b' form (the inactive form) is 5′AMP dependent, The two forms are developmentally regulated. Polyclortal antibodies raised to the purified forms of this enzyme show low cross reactivity. The anti-’a' antiserum reacts with a 104 kd protein that is associated with phosphorylase ’a' activity; the anti-’b' antiserum reacts with a 92 kd protein that is associated with phosphorylase ’b' activity and cross reacts weakly with the 104 kd protein. Cyclic AMP perturbation of intact cells caused induction of both phosphorylase ’a' activity and the appearance of the 104 kd protein. lmmunotitration data suggest that the ’a’ form accumulates due to de novo protein synthesis, although this result must be interpreted with caution. In vitro translation experiments indicate that separate mRNA species exist for the two forms of phosphorylase. The mRNA for the 'b’ form is present throughout development while that of the ’a' form appears late in development."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Master of Science"]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["The relationship between two forms of glycogen phosphorylase in Dictyostelium discoideum"]}]}],"canonical_facts":{"dc:contributor.department":["Biology"],"dc:creator":["Sucic, Joseph F."],"dc:date.accessioned":["2015-06-23T19:09:25Z"],"dc:date.available":["2015-06-23T19:09:25Z"],"dc:date.issued":["1988"],"dc:description.abstract":["The cellular slime mold, Dictyortelium dixcoideum, provides an ideal model system to study eukaryotic cell differentiation. In D. discoideum glycogen degradation provides precursors for the synthesis of developmentally regulated structural end products. The enzyme responsible for glycogen degradation, glycogen phosphorylase, exists in active and inactive forms. The activity of the ’a' form (the active form) is independent of 5′adenosine monophosphate (5′AMP) while the activity of the ’b' form (the inactive form) is 5′AMP dependent, The two forms are developmentally regulated. Polyclortal antibodies raised to the purified forms of this enzyme show low cross reactivity. The anti-’a' antiserum reacts with a 104 kd protein that is associated with phosphorylase ’a' activity; the anti-’b' antiserum reacts with a 92 kd protein that is associated with phosphorylase ’b' activity and cross reacts weakly with the 104 kd protein. Cyclic AMP perturbation of intact cells caused induction of both phosphorylase ’a' activity and the appearance of the 104 kd protein. lmmunotitration data suggest that the ’a’ form accumulates due to de novo protein synthesis, although this result must be interpreted with caution. In vitro translation experiments indicate that separate mRNA species exist for the two forms of phosphorylase. The mRNA for the 'b’ form is present throughout development while that of the ’a' form appears late in development."],"dc:description.degree":["Master of Science"],"dc:format.mimetype":["application/pdf"],"dc:identifier.uri":["http://hdl.handle.net/10919/53186"],"dc:language.iso":["en_US"],"dc:publisher":["Virginia Polytechnic Institute and State University"],"dc:rights":["In Copyright"],"dc:rights.uri":["http://rightsstatements.org/vocab/InC/1.0/"],"dc:title":["The relationship between two forms of glycogen phosphorylase in Dictyostelium discoideum"],"dc:type":["Thesis"],"dc:type.dcmitype":["Text"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["masters"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Virginia Polytechnic Institute and State University"]},"updated_at":"2026-07-22T22:19:37Z"}