| Autor: |
Braunwalder, Albert F., Yarwood, Donna R., Hall, Tony, Missbach, Martin, Lipson, Kenneth E., Sills, Matthew A. |
| Zdroj: |
Analytical Biochemistry; February 1996, Vol. 234 Issue: 1 p23-26, 4p |
| Abstrakt: |
A solid-phase assay for the determination of protein tyrosine kinase (PTK) activity has been developed. The transfer of33PO4from ATP to the synthetic substrate poly(Glu, Tyr) 4:1 attached to the bioactive surface of scintillating microtiter plates served as the basis to evaluate enzyme activity. The procedure eliminates detection with phosphotyrosine antibodies, tedious separation of phosphorylated peptides with phosphocellulose membranes, and extensive washing steps. For these reasons, the traditionally time-consuming procedure can be performed with a simple three-step protocol. The method is highly accurate, rapid, and robotics friendly. The advantages over existing assays make this procedure especially suited for high throughput applications. |
| Databáze: |
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| Externí odkaz: |
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