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Isolation of buffalo muscle aldolase ec 4.1.2.13 and comparison of its properties with those of rabbit muscle aldolase


, : Isolation of buffalo muscle aldolase ec 4.1.2.13 and comparison of its properties with those of rabbit muscle aldolase. Biochimica et Biophysica Acta 483(2): 435-442

Fructose-1,6-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate -lyase, EC 4.1.2.13) was isolated from buffalo muscle by fractionation with ammonium sulfate and subsequent purification by phosphocellulose column chromatography using a linear salt gradient. As judged by gel filtration and electrophoresis in polyacrylamide gel, the enzyme was homogeneous with respect to size and charge. The MW and Stokes radius of the enzyme were determined from its elution profile on a calibrated Sephadex column and the respective values were 162,000 and 4.55 nm. The diffusion coefficient and frictional ratio were computed to be 4.8 .cntdot. 10-7 cm2 .cntdot. s-1 and 1.27, respectively. The MW of the polypeptide chain as measured by sodium dodecyl sulfate polyacrylamide gel electrophoresis was 40,750. This taken together with the native MW suggested a 4-subunit model for the protein. The N- and C-terminal residues of polypeptide chains were identified to be proline and tyrosine, respectively. At pH 8.0 the Km and maximum attainable velocity were 8.1 .mu.M and 27 .mu.M Fru-1,6-P2 [fructose 1,6-bisphosphate] split/min mg, respectively. The buffalo muscle aldolase was similar to rabbit muscle aldolase in physicochemical properties. The 2 enzymes differ significantly in pH optimum; the pH optima of the buffalo and rabbit enzymes were determined under identical conditions to be 8.0 and 8.6, respectively.

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