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Alkaline phosphatase in Asterias bispinosa: Partial purification and characterization

โœ Scribed by Aisa, Elio; Aisa, M.Cristina; Ambrosini, M.Vittoria; Giovannini, Elvio

Book ID
122878959
Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
244 KB
Volume
72
Category
Article
ISSN
1096-4959

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Purification and partial characterizatio
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The I variant of placental alkaline phosphatase was purified to homogeneity by means of DEAE-cellulose chromatography, isoelectric focusing, and gel filtration on AcA-34. The specific activity of the I variant was found to be 3.33 micronkat/mg. The enzyme is a dimer with an isoelectric point of 4.6

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The two most common variants of placental alkaline phosphatase, the F and S variants, were purified to homogeneity and characterized. Their molecular weights were determined by equilibrium ultracentrifugation and sodium dodecylsufate polyacrylamide gel electrophoresis, which gave almost identical va