Purification and characterization of glutamate dehydrogenase from eel liver.

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  • ウナギ肝臓のグルタミン酸脱水素酵素の精製とその性質
  • ウナギ肝臓のグルタミン酸脱水素酵素の精製とその性質〔英文〕
  • ウナギ カンゾウ ノ グルタミンサン ダツ スイソ コウソ ノ セイセイ ト

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Glutamate dehydrogenase (EC 1.4.1.2-4) has been purified from the acetone powder of eel 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.<br> Sedimentation analysis gave a S020, w value of 12.3. The enzyme had a molecular weight of 315, 000, as determined by polyacrylamide gel electrophoresis.<br> 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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