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
Alkaline phosphatase ofDrosophila melanogaster. I. Partial purification and characterization
β Scribed by Robert A. Harper; F. B. Armstrong
- Publisher
- Springer
- Year
- 1972
- Tongue
- English
- Weight
- 488 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0006-2928
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