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
Hauptverfasser: Hayashi, S, Ise, K, Itakura, T, Oshiro, Z. (Kagoshima Univ. (Japan). Faculty of Fisheries)
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creator Hayashi, S
Ise, K
Itakura, T
Oshiro, Z. (Kagoshima Univ. (Japan). Faculty of Fisheries)
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.
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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. 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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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