Abstract
Fructose bisphosphatase ( d-fructose-1,6-biphosphate 1-phosphohydrolase, EC 3.1.3.11) has been isolated in homogeneous form from rat muscle by a simple and convenient procedure, including adsorption on carboxymethylcellulose and substrate elution. The resultant enzyme preparation has a specific activity comparable to that of the enzymes isolated from rabbit liver, rabbit muscle and rat liver. The native relative molecular mass of the enzyme was estimated by sedimentation equilibrium centrifugation to be approx. 138 000, and the enzyme appears to be a tetramer containing subunits of M r approx. 34 500. The amino acid composition is distinctly different from that of the rabbit muscle, rabbit liver and rat liver enzymes. The purified enzyme contains no tryptophan and has a blocked amino terminal.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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