| http://purl.uniprot.org/citations/16668794 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16668794 | http://www.w3.org/2000/01/rdf-schema#comment | "To obtain a monospecific antibody against NADH-dependent glutamate synthase (NADH-GOGAT; EC 1.4.1.14), the enzyme was purified to homogeneity from cultured rice cells (Oryza sativa) with column chromatography using Butyl Toyopearl 650M, Sephacryl S-300, Blue Sepharose CL-6B, and Butyl Toyopearl 650S. The specific activity at the final stage of the purification was 9.8 micromoles of glutamate formed per minute per milligram of protein. The yield was 6.1% and purification was 815-fold. Analysis by denaturing gel electrophoresis revealed a single polypeptide with an apparent molecular weight of 196,000, similar to the value of 194,000 estimated for the native protein. Apparent K(m) values for l-glutamine, 2-oxoglutarate, and NADH were 811, 76, and 3.0 micromolar, respectively. Neither NADPH nor l-asparagine substituted for NADH and l-glutamine, respectively. The enzyme had its absorption maxima at 273, 373, and 440 nanometers with a shoulder at 475 nanometers, suggesting that the rice NADH-GOGAT is a flavoprotein. Monospecific antibody raised against NADH-GOGAT purified from the rice cells was obtained as the first instance for the enzyme in higher plants. Immunological analyses showed that the antibody for rice cell NADH-GOGAT reacted with only the enzyme in extracts from the cells. The anti-NADH-GOGAT antibody did not recognize the ferredoxin-GOGAT purified from rice leaves, and likewise the anti-rice leaf ferredoxin-GOGAT antibody did not react with the NADH-GOGAT purified from the cultured rice cells."xsd:string |
| http://purl.uniprot.org/citations/16668794 | http://purl.org/dc/terms/identifier | "doi:10.1104/pp.98.4.1317"xsd:string |
| http://purl.uniprot.org/citations/16668794 | http://purl.uniprot.org/core/author | "Hayakawa T."xsd:string |
| http://purl.uniprot.org/citations/16668794 | http://purl.uniprot.org/core/author | "Yamaya T."xsd:string |
| http://purl.uniprot.org/citations/16668794 | http://purl.uniprot.org/core/author | "Kamachi K."xsd:string |
| http://purl.uniprot.org/citations/16668794 | http://purl.uniprot.org/core/author | "Ojima K."xsd:string |
| http://purl.uniprot.org/citations/16668794 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/16668794 | http://purl.uniprot.org/core/name | "Plant Physiol"xsd:string |
| http://purl.uniprot.org/citations/16668794 | http://purl.uniprot.org/core/pages | "1317-1322"xsd:string |
| http://purl.uniprot.org/citations/16668794 | http://purl.uniprot.org/core/title | "Purification, Characterization, and Immunological Properties of NADH-Dependent Glutamate Synthase from Rice Cell Cultures."xsd:string |
| http://purl.uniprot.org/citations/16668794 | http://purl.uniprot.org/core/volume | "98"xsd:string |
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