Section 45
Chapter 44,106

Purification of skeletal muscle hexokinase by affinity elution chromatography

Qadri, S.S.; Easterby, J.S.

Analytical Biochemistry 105(2): 299-303


ISSN/ISBN: 0003-2697
PMID: 7457836
DOI: 10.1016/0003-2697(80)90461-3
Accession: 044105596

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Type Ii hexokinase (Ec has been purified from rat skeletal muscle by a simple procedure involving chromatography on DEAE-cellulose, affinity elution chromatography from phosphocellulose, and gel filtration on Sephadex G-200. The key to the preparation of homogeneous enzyme is the affinity elution step in which an effector molecule, glucose 6-phosphate, is used as the eluting ligand. A 5300-fold purification is obtained by the procedure and over 400-fold purification is obtained in the affinity elution step alone. Approximately 3.3 mg of homogeneous hexokinase with a specific activity of 120 units/mg is obtained from 800 g of rat limb.

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