Abstract
The goal was to optimise a purification procedure of adenosine deaminase from human erythrocytes for the preparation of a European Reference Material. Adenosine deaminase was purified from human erythrocytes with a specific activity of 4.46 μkat/mg of protein and a catalytic concentration of 133 μkat/l. The isolation and purification procedure involved ion-exchange chromatography (STREAMLINE(TM) DEAE), and two purine riboside affinity chromatographies. The purified enzyme exhibits a single band in SDS-PAGE with a molecular weight of 41 600 g/mol, and three bands in PAGE, isoelectric focusing and two-dimensional electrophoresis with pI 4.7, 4.85 and 5.0. © 2000 Elsevier Science B.V.
Original language | English |
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Pages (from-to) | 237-244 |
Journal | Journal of Chromatography B: Biomedical Sciences and Applications |
Volume | 737 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 14 Jan 2000 |
Keywords
- Adenosine deaminase
- Enzymes
- Purification