Purification and Characterization of Aldolase From Ambystoma Tigrinum
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 Sephade...
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| Format: | Others |
| Language: | English |
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North Texas State University
1975
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| Online Access: | https://digital.library.unt.edu/ark:/67531/metadc798290/ |
| Summary: | 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 electrophoresis and is apparently a tetramer of nearly identical subunits of approximately 40,000 MW. The catalytic constants of the salamander enzyme were similar to those reported for other muscle aldolases with the exception of the unusually low Fru-P2/FlP ratio. |
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