Isolation and partial characterization of rat muscle fructose biphosphatase

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 acti...

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Published inBiochimica et biophysica acta, Protein structure and molecular enzymology Vol. 831; no. 2; pp. 186 - 191
Main Authors van Tonder, André, Terblanche, Stephanus E., Oelofsen, Willem
Format Journal Article
LanguageEnglish
Published Elsevier B.V 04.10.1985
Subjects
Amino acid composition
Fructose bisphosphatase
Rat skeletal muscle
Substrate specificity
Fructose bisphosphatase
Amino acid composition
Substrate specificity
Rat skeletal muscle
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Summary: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.
ISSN:0167-4838
1879-2588
DOI:10.1016/0167-4838(85)90034-2