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• W2015217773 abstract "1. Fructose-1,6-diphosphate aldolase has been purified from the muscle tissue of the roundworm, Ascaris suum. 2. The 157-fold purified enzymes exhibits a specific activity of 10·2 units/mg of protein and was judge to be homogeneous by the criteria of analytical ultracentrifugation, zone electrophoresis and rechromatography. 3. Concomitant with the homogeneity studies the following physical parameters were established: S020,wW=7·98x10−13sec; D20,ww=4·43x10−7cm2/sec; Strokes' radius=46·4 Å; f/f0=1·29. 4. Sedimentation velocity and sedimentation equilibrium ultracentrifugation and analytical gel filtration yielded a molecular weight of 158,000±4000 for the native enzymes. The subunit molecular weight in 6 M guanidinium chloride or 0·1% sodium dodecyl sulfate is 41,000. Therefore, the enzyme is a tetramer. 5. The apparent Michaelis constants determined for FDP and F1P were 6x10−5M and 3x10−2M, respectively. The catalytic ratio (FDP/F1P) was 42. The enzymes was unaffected by EDTA or potassium ions. 6. It is concluded that the enzyme is a typical Class I, Type A muscle aldolase, and is suprisingly similar to the muscle aldolase of vertebrate origin." @default.
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• W2015217773 date "1973-01-01" @default.
• W2015217773 modified "2023-10-16" @default.
• W2015217773 title "Studies on enzymes from parasitic helminths—IV. Purification and characterization of aldolase from the muscle tissue of Ascaris suum" @default.
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• W2015217773 doi "https://doi.org/10.1016/0305-0491(73)90366-0" @default.
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