Purification of human adenosine deaminase for the preparation of a reference material

Alexandre Bota; F. Javier Gella; Francesca Canalias

doi:10.1016/S0378-4347(99)00359-X

Purification of human adenosine deaminase for the preparation of a reference material

Alexandre Bota, F. Javier Gella, Francesca Canalias

Department of Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › Research › peer-review

7 Citations (Scopus)

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
Pages (from-to)	237-244
Journal	Journal of Chromatography B: Biomedical Sciences and Applications
Volume	737
Issue number	1-2
DOIs	https://doi.org/10.1016/S0378-4347(99)00359-X
Publication status	Published - 14 Jan 2000

Keywords

Adenosine deaminase
Enzymes
Purification

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10.1016/S0378-4347(99)00359-X

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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. {\textcopyright} 2000 Elsevier Science B.V.",

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AU - Gella, F. Javier

AU - Canalias, Francesca

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N2 - 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.

AB - 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.

KW - Adenosine deaminase

KW - Enzymes

KW - Purification

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M3 - Article

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SP - 237

EP - 244

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ER -

Purification of human adenosine deaminase for the preparation of a reference material

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Keywords

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