Rapid purification of adenylate kinase from human erythrocytes and skeletal muscle
Adenylate kinase from human erythrocytes and skeletal muscle can be purified to homogeneity by a new procedure based on DEAE-Sepharose and Blue Sepharose affinity chromatography and Sephadex G-75 fractionation. For the enzyme purified from erythrocytes the specific activity is 3000 U/mg of protein,...
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Veröffentlicht in: | Archives of biochemistry and biophysics 1986-10, Vol.250 (1), p.19-22 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Adenylate kinase from human erythrocytes and skeletal muscle can be purified to homogeneity by a new procedure based on DEAE-Sepharose and Blue Sepharose affinity chromatography and Sephadex G-75 fractionation. For the enzyme purified from erythrocytes the specific activity is 3000 U/mg of protein, and the overall yield is 70%. For the enzyme purified from skeletal muscle the specific activity is 2075 U/mg of protein, and the overall yield is 44%. The sequence of steps takes advantage of the high isoelectric point, the high affinity for Blue Sepharose, and the low molecular weight of the isoenzyme from these two human tissues. |
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ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1016/0003-9861(86)90696-X |