Partial purification and characterization of a soluble protein phosphatase fromLeishmania donovanipromastigotes
โ Scribed by Srabani Nandi; Dwijen Sarkar
- Publisher
- Springer
- Year
- 1995
- Tongue
- English
- Weight
- 745 KB
- Volume
- 148
- Category
- Article
- ISSN
- 0300-8177
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๐ SIMILAR VOLUMES
PTP-MEG2 is an intracellular protein tyrosine phosphatase with a putative lipid-binding domain at the N-terminus. The present study reports expression, purification, and characterization of the full-length form of the enzyme plus a truncated form containing the catalytic domain alone. Full-length PT
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