| Autor: |
Carlino, A., Toledo, H., Vidal, V., Redfield, B., Strassman, J., Abdelghany, M., Racker, E., Weissbach, H., Brot, N. |
| Zdroj: |
Biochemical and Biophysical Research Communications; June 30, 1994, Vol. 201 Issue: 3 p1548-1553, 6p |
| Abstrakt: |
In a study to investigate the ability of chaperones to modulate src kinase activity, it was observed that BiP, a member of the HSP70 family found in the endoplasmic reticulum, is an excellent substrate for src kinase in vitro. The reaction requires polylysine and the results suggest that two tyrosine residues are phosphorylated. Although there is no evidence for this reaction in vivo, it does provide a very efficient method to label BiP.Copyright 1994, 1999 Academic Press, Inc. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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