{"id":{"repo_id":"vt","oai_identifier":"oai:vtechworks.lib.vt.edu:10919/53601"},"canonical_url":"https://search.dev.ndltd.org/etd/vt/oai:vtechworks.lib.vt.edu:10919/53601","repository":{"repo_id":"vt","name":"Virginia Tech","base_url":"https://vtechworks.lib.vt.edu/oai/request"},"display":{"title":"Studies on maize beta glucosidase gene-enzyme system","abstract":"Maize ß-glucosidase is implicated in phytohormone catabolism, disease resistance mechanisms, and also the catabolism of various ß-D-glucosides. The enzyme expressed in maize sporophytes is encoded by a highly polymorphic locus, Glul (chromosome 10). In the present study, maize ß-glucosidase was purified to homogeneity by using differential solubility and chromatography. The enzyme is soluble and synthesized adaptively after germination. The isoelectric point (pl) of the native enzyme is 4.9-5.0 and its temperature and pH optima are 40°C and 6.8, respectively. The active enzyme is temperature·sensitive and composed of two identical, non-covalently associated and catalytically inactive polypeptides (60 kD each). Enzyme catalysis shows dominant aryl ß-glucosidase and ß-fucosidase activities compared to cellobiase activity. Activity is (1) influenced by the configuration of the C-4 and C-6 atoms on the glycone moeity and by the substrate chain length, (2) possibly mediated by an imidazole ring and a terminal α-amino group in the enzyme catalytic and binding sites, respectively, (3) dependent on intra-chain disulfide bonds to maintain the enzyme conformation, and (4) inhibited competitively by the end product, glucose. The sporophytic specificity of Glul expression might be controlled by tightly linked cis- and trans- acting regulatory elements. One of the several null mutations, with an apparent allelism to Glul locus, (l) complements in trans when combined with normal Glul alleles, and (2) probably affects a shift in the tissue-specific expression of Glul locus (from sporophytic to gametophytic). Another structural gene, GIu3, encoding a soluble, sporophyte-specific, and electrophoretically-invariant ß-glucosidase isoenzyme is present based on hydrodynamic properties, size, surface net charge, peptide map, quaternary structure, and enzyme kinetics.","abstract_html":"Maize ß-glucosidase is implicated in phytohormone catabolism, disease resistance mechanisms, and also the catabolism of various ß-D-glucosides. The enzyme expressed in maize sporophytes is encoded by a highly polymorphic locus, Glul (chromosome 10). In the present study, maize ß-glucosidase was purified to homogeneity by using differential solubility and chromatography. The enzyme is soluble and synthesized adaptively after germination. The isoelectric point (pl) of the native enzyme is 4.9-5.0 and its temperature and pH optima are 40°C and 6.8, respectively. The active enzyme is temperature·sensitive and composed of two identical, non-covalently associated and catalytically inactive polypeptides (60 kD each). Enzyme catalysis shows dominant aryl ß-glucosidase and ß-fucosidase activities compared to cellobiase activity. Activity is (1) influenced by the configuration of the C-4 and C-6 atoms on the glycone moeity and by the substrate chain length, (2) possibly mediated by an imidazole ring and a terminal α-amino group in the enzyme catalytic and binding sites, respectively, (3) dependent on intra-chain disulfide bonds to maintain the enzyme conformation, and (4) inhibited competitively by the end product, glucose. The sporophytic specificity of Glul expression might be controlled by tightly linked cis- and trans- acting regulatory elements. One of the several null mutations, with an apparent allelism to Glul locus, (l) complements in trans when combined with normal Glul alleles, and (2) probably affects a shift in the tissue-specific expression of Glul locus (from sporophytic to gametophytic). Another structural gene, GIu3, encoding a soluble, sporophyte-specific, and electrophoretically-invariant ß-glucosidase isoenzyme is present based on hydrodynamic properties, size, surface net charge, peptide map, quaternary structure, and enzyme kinetics.","abstract_has_math":false,"creators":["Rifaat, Mahmoud M."],"institution":"Virginia Polytechnic Institute and State University","degree_name":"Ph. D.","degree_level":"doctoral","degree_discipline":"Genetics","degree_department":"Genetics","school":null,"contributors":[],"advisors":[],"committee_chairs":["Esen, Asim"],"committee_members":["Bates, Robert C.","Falkinham, Joseph O. III","Johnson, John L.","Wallace, Bruce"],"year":1988,"date_issued":"1988","date_published":"1988","updated_at":"2026-07-22T22:20:08Z","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/10919/53601","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.committeechair","label":"Committee Chair","values":["Esen, Asim"]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Bates, Robert C.","Falkinham, Joseph O. 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In the present study, maize ß-glucosidase was purified to homogeneity by using differential solubility and chromatography. The enzyme is soluble and synthesized adaptively after germination. The isoelectric point (pl) of the native enzyme is 4.9-5.0 and its temperature and pH optima are 40°C and 6.8, respectively. The active enzyme is temperature·sensitive and composed of two identical, non-covalently associated and catalytically inactive polypeptides (60 kD each). Enzyme catalysis shows dominant aryl ß-glucosidase and ß-fucosidase activities compared to cellobiase activity. Activity is (1) influenced by the configuration of the C-4 and C-6 atoms on the glycone moeity and by the substrate chain length, (2) possibly mediated by an imidazole ring and a terminal α-amino group in the enzyme catalytic and binding sites, respectively, (3) dependent on intra-chain disulfide bonds to maintain the enzyme conformation, and (4) inhibited competitively by the end product, glucose. The sporophytic specificity of Glul expression might be controlled by tightly linked cis- and trans- acting regulatory elements. One of the several null mutations, with an apparent allelism to Glul locus, (l) complements in trans when combined with normal Glul alleles, and (2) probably affects a shift in the tissue-specific expression of Glul locus (from sporophytic to gametophytic). Another structural gene, GIu3, encoding a soluble, sporophyte-specific, and electrophoretically-invariant ß-glucosidase isoenzyme is present based on hydrodynamic properties, size, surface net charge, peptide map, quaternary structure, and enzyme kinetics."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Ph. D."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Studies on maize beta glucosidase gene-enzyme system"]}]}],"canonical_facts":{"dc:contributor.committeechair":["Esen, Asim"],"dc:contributor.committeemember":["Bates, Robert C.","Falkinham, Joseph O. III","Johnson, John L.","Wallace, Bruce"],"dc:contributor.department":["Genetics"],"dc:creator":["Rifaat, Mahmoud M."],"dc:date.accessioned":["2015-06-24T13:35:20Z"],"dc:date.available":["2015-06-24T13:35:20Z"],"dc:date.issued":["1988"],"dc:description.abstract":["Maize ß-glucosidase is implicated in phytohormone catabolism, disease resistance mechanisms, and also the catabolism of various ß-D-glucosides. The enzyme expressed in maize sporophytes is encoded by a highly polymorphic locus, Glul (chromosome 10). In the present study, maize ß-glucosidase was purified to homogeneity by using differential solubility and chromatography. The enzyme is soluble and synthesized adaptively after germination. The isoelectric point (pl) of the native enzyme is 4.9-5.0 and its temperature and pH optima are 40°C and 6.8, respectively. The active enzyme is temperature·sensitive and composed of two identical, non-covalently associated and catalytically inactive polypeptides (60 kD each). Enzyme catalysis shows dominant aryl ß-glucosidase and ß-fucosidase activities compared to cellobiase activity. Activity is (1) influenced by the configuration of the C-4 and C-6 atoms on the glycone moeity and by the substrate chain length, (2) possibly mediated by an imidazole ring and a terminal α-amino group in the enzyme catalytic and binding sites, respectively, (3) dependent on intra-chain disulfide bonds to maintain the enzyme conformation, and (4) inhibited competitively by the end product, glucose. The sporophytic specificity of Glul expression might be controlled by tightly linked cis- and trans- acting regulatory elements. One of the several null mutations, with an apparent allelism to Glul locus, (l) complements in trans when combined with normal Glul alleles, and (2) probably affects a shift in the tissue-specific expression of Glul locus (from sporophytic to gametophytic). Another structural gene, GIu3, encoding a soluble, sporophyte-specific, and electrophoretically-invariant ß-glucosidase isoenzyme is present based on hydrodynamic properties, size, surface net charge, peptide map, quaternary structure, and enzyme kinetics."],"dc:description.degree":["Ph. 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