| Autor: |
L, Sivanaesan, T K, Kwan, R, Perumal |
| Rok vydání: |
1991 |
| Předmět: |
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| Zdroj: |
Biochemistry international. 25(3) |
| ISSN: |
0158-5231 |
| Popis: |
Calmodulin, an activator protein in most calcium-dependent processes, was isolated to apparent homogeneity from the femurs of 1-day old chicks using phenyl-Sepharose and high performance liquid chromatography. The purified calmodulin was found to produce a 6-fold increase in the activity of alkaline phosphatase isolated from the same source. A Ca2+ concentration of 10(-5) M was required for the activation. Purification of alkaline phosphatase involved acetone precipitation, DEAE-Sephacel and Sephadex G-200 column chromatography. The enzyme was purified to 540-fold and had a specific activity of 10.75 U/mg protein. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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