Purification and Characterization of Aldolase From Ambystoma Tigrinum
Description:
The muscle aldolase from Ambystoma tigrinum has been purified 73-fold to a final specific activity of 13.2 units per mg. The purified enzyme appeared to be homogenous by ultracentrifugation and electrophoretic criteria. A molecular weight of 159,000 + 1000 was determined by gel filtration on Sephadex G-200 and high speed sedimentation equilibrium ultracentrifugation. The enzyme migrated identically with rabbit muscle aldolase when subjected to sodium dodecyl sulfate polyacrylamide gel electroph…
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Date:
December 1975
Creator:
Woolever, Dorothy J.
Partner:
UNT Libraries