Purification and partial characterization of the placental-like alkaline phosphatase in human lung tissue
โ Scribed by Kazuyuki Hirano; Iwao Koyama; Torgny Stigbrand
- Book ID
- 115826730
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 664 KB
- Volume
- 186
- Category
- Article
- ISSN
- 0009-8981
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๐ SIMILAR VOLUMES
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
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