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
1. Verfasser: Nealon, Daniel A.
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.
ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(86)90696-X