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...
Main Author: | Woolever, Dorothy J. |
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Format: | Others |
Language: | English |
Published: |
North Texas State University
1975
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Subjects: | |
Online Access: | https://digital.library.unt.edu/ark:/67531/metadc798290/ |
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