Purification and characterization of glutamate dehydrogenase from eel liver
Glutamate dehydrogenase (EC 1.4.1.2-4) has been purified from the acetone powder of eel (Anguilla japonica ) liver; the process utilized affinity chromatography with GTP-Sepharose in the final step. The homogeneity of the enzyme was proved by 1) a single protein-staining band in polyacrylamide gels,...
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Veröffentlicht in: | Nippon Suisan Gakkaishi 1982-01, Vol.48 (4), p.557-562 |
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description | Glutamate dehydrogenase (EC 1.4.1.2-4) has been purified from the acetone powder of eel (Anguilla japonica ) liver; the process utilized affinity chromatography with GTP-Sepharose in the final step. The homogeneity of the enzyme was proved by 1) a single protein-staining band in polyacrylamide gels, 2) a single symmetrical Schlieren peak in the ultracentrifuge, and 3) constant specific activity in the chromatogram obtained by GTP-Sepharose column. Sedimentation analysis gave a S degree sub(2)0,wv)alue of 12.3. The enzyme had a molecular weight of 315,000. In gel electrophoresis, the enzyme showed little mobility if ADP was not added in sample, spacer and separate gel. Amino acid analysis showed that the ratio of quantities of arginine, lysine, and tyrosine to the total residues of amino acids in the eel enzyme were rather higher than those in bovine, rat, and tuna enzymes. |
doi_str_mv | 10.2331/suisan.48.557 |
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(Kagoshima Univ. (Japan). Faculty of Fisheries)</creator><creatorcontrib>Hayashi, S ; Ise, K ; Itakura, T ; Oshiro, Z. (Kagoshima Univ. (Japan). Faculty of Fisheries)</creatorcontrib><description>Glutamate dehydrogenase (EC 1.4.1.2-4) has been purified from the acetone powder of eel (Anguilla japonica ) liver; the process utilized affinity chromatography with GTP-Sepharose in the final step. The homogeneity of the enzyme was proved by 1) a single protein-staining band in polyacrylamide gels, 2) a single symmetrical Schlieren peak in the ultracentrifuge, and 3) constant specific activity in the chromatogram obtained by GTP-Sepharose column. Sedimentation analysis gave a S degree sub(2)0,wv)alue of 12.3. The enzyme had a molecular weight of 315,000. In gel electrophoresis, the enzyme showed little mobility if ADP was not added in sample, spacer and separate gel. Amino acid analysis showed that the ratio of quantities of arginine, lysine, and tyrosine to the total residues of amino acids in the eel enzyme were rather higher than those in bovine, rat, and tuna enzymes.</description><identifier>ISSN: 0021-5392</identifier><identifier>EISSN: 1349-998X</identifier><identifier>DOI: 10.2331/suisan.48.557</identifier><language>eng</language><subject>ALIMENTOS ; ANATOMIA ; ANATOMIA ANIMAL ; ANATOMIE ; ANATOMIE ANIMALE ; ANATOMY ; ANGUILA ; Anguilla japonica ; ANGUILLE ; Anguillidae ; ANIMAL ; ANIMAL ANATOMY ; ANIMAL AQUATIQUE ; ANIMALES ; ANIMALES ACUATICOS ; ANIMALS ; APPAREIL DIGESTIF ; AQUATIC ANIMALS ; AQUATIC ORGANISMS ; BODY PARTS ; CEIUAPA (GRUPO B-22) ; CEIUAPA (GRUPOS DE ESPECIES) ; CHEMICOPHYSICAL PROPERTIES ; COMPOSE ORGANIQUE ; COMPUESTOS ORGANICOS ; DIADROMOUS FISHES ; DIGESTIVE SYSTEM ; EELS ; ENZIMAS ; ENZYME ; ENZYMES ; EPURATION ; FISHES ; FOIE ; FOODS ; GROUPE B-22 DE LA CSITAPA ; GROUPE D'ESPECES DE LA CSITAPA ; HIGADO ; ISSCAAP GROUP B-22 ; ISSCAAP GROUPS OF SPECIES ; LIVER ; ORGANIC COMPOUNDS ; ORGANISME AQUATIQUE ; ORGANISMOS ACUATICOS ; OXIDOREDUCTASES ; OXIDORREDUCTASAS ; OXYDOREDUCTASE ; PARTES DEL CUERPO ; PARTIE DU CORPS ; PECES ; PECES DIADROMOS ; POISSON ; POISSON DIADROME ; PROCESAMIENTO ; PROCESSING ; PRODUIT ALIMENTAIRE ; PROPIEDADES FISICO-QUIMICAS ; PROPRIETE PHYSICO-CHIMIQUE ; PURIFICACION ; PURIFICATION ; SISTEMA DIGESTIVO ; TRAITEMENT ; VERTEBRADOS ; VERTEBRATES ; VERTEBRE</subject><ispartof>Nippon Suisan Gakkaishi, 1982-01, Vol.48 (4), p.557-562</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids></links><search><creatorcontrib>Hayashi, S</creatorcontrib><creatorcontrib>Ise, K</creatorcontrib><creatorcontrib>Itakura, T</creatorcontrib><creatorcontrib>Oshiro, Z. (Kagoshima Univ. (Japan). Faculty of Fisheries)</creatorcontrib><title>Purification and characterization of glutamate dehydrogenase from eel liver</title><title>Nippon Suisan Gakkaishi</title><description>Glutamate dehydrogenase (EC 1.4.1.2-4) has been purified from the acetone powder of eel (Anguilla japonica ) liver; the process utilized affinity chromatography with GTP-Sepharose in the final step. The homogeneity of the enzyme was proved by 1) a single protein-staining band in polyacrylamide gels, 2) a single symmetrical Schlieren peak in the ultracentrifuge, and 3) constant specific activity in the chromatogram obtained by GTP-Sepharose column. Sedimentation analysis gave a S degree sub(2)0,wv)alue of 12.3. The enzyme had a molecular weight of 315,000. In gel electrophoresis, the enzyme showed little mobility if ADP was not added in sample, spacer and separate gel. Amino acid analysis showed that the ratio of quantities of arginine, lysine, and tyrosine to the total residues of amino acids in the eel enzyme were rather higher than those in bovine, rat, and tuna enzymes.</description><subject>ALIMENTOS</subject><subject>ANATOMIA</subject><subject>ANATOMIA ANIMAL</subject><subject>ANATOMIE</subject><subject>ANATOMIE ANIMALE</subject><subject>ANATOMY</subject><subject>ANGUILA</subject><subject>Anguilla japonica</subject><subject>ANGUILLE</subject><subject>Anguillidae</subject><subject>ANIMAL</subject><subject>ANIMAL ANATOMY</subject><subject>ANIMAL AQUATIQUE</subject><subject>ANIMALES</subject><subject>ANIMALES ACUATICOS</subject><subject>ANIMALS</subject><subject>APPAREIL DIGESTIF</subject><subject>AQUATIC ANIMALS</subject><subject>AQUATIC ORGANISMS</subject><subject>BODY PARTS</subject><subject>CEIUAPA (GRUPO B-22)</subject><subject>CEIUAPA (GRUPOS DE ESPECIES)</subject><subject>CHEMICOPHYSICAL PROPERTIES</subject><subject>COMPOSE ORGANIQUE</subject><subject>COMPUESTOS ORGANICOS</subject><subject>DIADROMOUS FISHES</subject><subject>DIGESTIVE SYSTEM</subject><subject>EELS</subject><subject>ENZIMAS</subject><subject>ENZYME</subject><subject>ENZYMES</subject><subject>EPURATION</subject><subject>FISHES</subject><subject>FOIE</subject><subject>FOODS</subject><subject>GROUPE B-22 DE LA CSITAPA</subject><subject>GROUPE D'ESPECES DE LA CSITAPA</subject><subject>HIGADO</subject><subject>ISSCAAP GROUP B-22</subject><subject>ISSCAAP GROUPS OF SPECIES</subject><subject>LIVER</subject><subject>ORGANIC COMPOUNDS</subject><subject>ORGANISME AQUATIQUE</subject><subject>ORGANISMOS ACUATICOS</subject><subject>OXIDOREDUCTASES</subject><subject>OXIDORREDUCTASAS</subject><subject>OXYDOREDUCTASE</subject><subject>PARTES DEL CUERPO</subject><subject>PARTIE DU CORPS</subject><subject>PECES</subject><subject>PECES DIADROMOS</subject><subject>POISSON</subject><subject>POISSON DIADROME</subject><subject>PROCESAMIENTO</subject><subject>PROCESSING</subject><subject>PRODUIT ALIMENTAIRE</subject><subject>PROPIEDADES FISICO-QUIMICAS</subject><subject>PROPRIETE PHYSICO-CHIMIQUE</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>SISTEMA DIGESTIVO</subject><subject>TRAITEMENT</subject><subject>VERTEBRADOS</subject><subject>VERTEBRATES</subject><subject>VERTEBRE</subject><issn>0021-5392</issn><issn>1349-998X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><recordid>eNqF0DtPwzAUhmELgUQpjCxMmdhSfI3tEVXcK9EBJDbrxJfWKE2KnSCVX0-rsDMd6ejRN7wIXRI8o4yRmzzEDO2Mq5kQ8ghNCOO61Fp9HKMJxpSUgml6is5y_sSYSabYBL0shxRDtNDHri2gdYVdQwLb-xR_xmcXilUz9LCB3hfOr3cudSvfQvZFSN2m8L4pmvjt0zk6CdBkf_F3p-j9_u5t_lguXh-e5reL0jLC-pIFXXOsvK4rK2rgtQ_cMQFOEs6oZEEELXWtqdJUgnIEODhRWVdhrmjgbIqux91t6r4Gn3uzidn6poHWd0M2RHAtpVT_QyY0JvgAyxHa1OWcfDDbFDeQdoZgc2hrxraGK7Nvu_dXow_QGVilmM3zUlFcSSHYLwdOd0U</recordid><startdate>19820101</startdate><enddate>19820101</enddate><creator>Hayashi, S</creator><creator>Ise, K</creator><creator>Itakura, T</creator><creator>Oshiro, Z. (Kagoshima Univ. (Japan). Faculty of Fisheries)</creator><scope>FBQ</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7TN</scope></search><sort><creationdate>19820101</creationdate><title>Purification and characterization of glutamate dehydrogenase from eel liver</title><author>Hayashi, S ; Ise, K ; Itakura, T ; Oshiro, Z. (Kagoshima Univ. (Japan). Faculty of Fisheries)</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c313t-3f9b408e9b6c5ba4bef4d35ad7143273f5f979b928927a8d1a4ad56cd60482f43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>ALIMENTOS</topic><topic>ANATOMIA</topic><topic>ANATOMIA ANIMAL</topic><topic>ANATOMIE</topic><topic>ANATOMIE ANIMALE</topic><topic>ANATOMY</topic><topic>ANGUILA</topic><topic>Anguilla japonica</topic><topic>ANGUILLE</topic><topic>Anguillidae</topic><topic>ANIMAL</topic><topic>ANIMAL ANATOMY</topic><topic>ANIMAL AQUATIQUE</topic><topic>ANIMALES</topic><topic>ANIMALES ACUATICOS</topic><topic>ANIMALS</topic><topic>APPAREIL DIGESTIF</topic><topic>AQUATIC ANIMALS</topic><topic>AQUATIC ORGANISMS</topic><topic>BODY PARTS</topic><topic>CEIUAPA (GRUPO B-22)</topic><topic>CEIUAPA (GRUPOS DE ESPECIES)</topic><topic>CHEMICOPHYSICAL PROPERTIES</topic><topic>COMPOSE ORGANIQUE</topic><topic>COMPUESTOS ORGANICOS</topic><topic>DIADROMOUS FISHES</topic><topic>DIGESTIVE SYSTEM</topic><topic>EELS</topic><topic>ENZIMAS</topic><topic>ENZYME</topic><topic>ENZYMES</topic><topic>EPURATION</topic><topic>FISHES</topic><topic>FOIE</topic><topic>FOODS</topic><topic>GROUPE B-22 DE LA CSITAPA</topic><topic>GROUPE D'ESPECES DE LA CSITAPA</topic><topic>HIGADO</topic><topic>ISSCAAP GROUP B-22</topic><topic>ISSCAAP GROUPS OF SPECIES</topic><topic>LIVER</topic><topic>ORGANIC COMPOUNDS</topic><topic>ORGANISME AQUATIQUE</topic><topic>ORGANISMOS ACUATICOS</topic><topic>OXIDOREDUCTASES</topic><topic>OXIDORREDUCTASAS</topic><topic>OXYDOREDUCTASE</topic><topic>PARTES DEL CUERPO</topic><topic>PARTIE DU CORPS</topic><topic>PECES</topic><topic>PECES DIADROMOS</topic><topic>POISSON</topic><topic>POISSON DIADROME</topic><topic>PROCESAMIENTO</topic><topic>PROCESSING</topic><topic>PRODUIT ALIMENTAIRE</topic><topic>PROPIEDADES FISICO-QUIMICAS</topic><topic>PROPRIETE PHYSICO-CHIMIQUE</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>SISTEMA DIGESTIVO</topic><topic>TRAITEMENT</topic><topic>VERTEBRADOS</topic><topic>VERTEBRATES</topic><topic>VERTEBRE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hayashi, S</creatorcontrib><creatorcontrib>Ise, K</creatorcontrib><creatorcontrib>Itakura, T</creatorcontrib><creatorcontrib>Oshiro, Z. (Kagoshima Univ. (Japan). Faculty of Fisheries)</creatorcontrib><collection>AGRIS</collection><collection>CrossRef</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Oceanic Abstracts</collection><jtitle>Nippon Suisan Gakkaishi</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hayashi, S</au><au>Ise, K</au><au>Itakura, T</au><au>Oshiro, Z. (Kagoshima Univ. (Japan). Faculty of Fisheries)</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of glutamate dehydrogenase from eel liver</atitle><jtitle>Nippon Suisan Gakkaishi</jtitle><date>1982-01-01</date><risdate>1982</risdate><volume>48</volume><issue>4</issue><spage>557</spage><epage>562</epage><pages>557-562</pages><issn>0021-5392</issn><eissn>1349-998X</eissn><abstract>Glutamate dehydrogenase (EC 1.4.1.2-4) has been purified from the acetone powder of eel (Anguilla japonica ) liver; the process utilized affinity chromatography with GTP-Sepharose in the final step. The homogeneity of the enzyme was proved by 1) a single protein-staining band in polyacrylamide gels, 2) a single symmetrical Schlieren peak in the ultracentrifuge, and 3) constant specific activity in the chromatogram obtained by GTP-Sepharose column. Sedimentation analysis gave a S degree sub(2)0,wv)alue of 12.3. The enzyme had a molecular weight of 315,000. In gel electrophoresis, the enzyme showed little mobility if ADP was not added in sample, spacer and separate gel. Amino acid analysis showed that the ratio of quantities of arginine, lysine, and tyrosine to the total residues of amino acids in the eel enzyme were rather higher than those in bovine, rat, and tuna enzymes.</abstract><doi>10.2331/suisan.48.557</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | ALIMENTOS ANATOMIA ANATOMIA ANIMAL ANATOMIE ANATOMIE ANIMALE ANATOMY ANGUILA Anguilla japonica ANGUILLE Anguillidae ANIMAL ANIMAL ANATOMY ANIMAL AQUATIQUE ANIMALES ANIMALES ACUATICOS ANIMALS APPAREIL DIGESTIF AQUATIC ANIMALS AQUATIC ORGANISMS BODY PARTS CEIUAPA (GRUPO B-22) CEIUAPA (GRUPOS DE ESPECIES) CHEMICOPHYSICAL PROPERTIES COMPOSE ORGANIQUE COMPUESTOS ORGANICOS DIADROMOUS FISHES DIGESTIVE SYSTEM EELS ENZIMAS ENZYME ENZYMES EPURATION FISHES FOIE FOODS GROUPE B-22 DE LA CSITAPA GROUPE D'ESPECES DE LA CSITAPA HIGADO ISSCAAP GROUP B-22 ISSCAAP GROUPS OF SPECIES LIVER ORGANIC COMPOUNDS ORGANISME AQUATIQUE ORGANISMOS ACUATICOS OXIDOREDUCTASES OXIDORREDUCTASAS OXYDOREDUCTASE PARTES DEL CUERPO PARTIE DU CORPS PECES PECES DIADROMOS POISSON POISSON DIADROME PROCESAMIENTO PROCESSING PRODUIT ALIMENTAIRE PROPIEDADES FISICO-QUIMICAS PROPRIETE PHYSICO-CHIMIQUE PURIFICACION PURIFICATION SISTEMA DIGESTIVO TRAITEMENT VERTEBRADOS VERTEBRATES VERTEBRE |
title | Purification and characterization of glutamate dehydrogenase from eel liver |
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