Phosphate Group-Derivated Bipyridine–Ruthenium Complex and Titanium Dioxide Nanoparticles for Electrochemical Sensing of Protein Kinase Activity

ACS Sensors ◽  
2021 ◽  
Author(s):  
Ge Zhang ◽  
Jingwen Liu ◽  
Chengying Liu ◽  
Fan Ding ◽  
Yingqian Li ◽  
...  
1976 ◽  
Vol 35 (03) ◽  
pp. 635-642 ◽  
Author(s):  
M Steiner

SummaryThe effect of thrombin on the phosphorylating activity of platelet membranes was compared to that of trypsin. Preincubation of non-32P phosphorylated platelet membranes with or without either of these two enzymes resulted in a considerable loss of membrane protein kinase activity which was most severe when trypsin was used. Protein kinase activity and endogenous protein acceptors decreased in parallel. 32P-phosphorylated membranes showed a slow but progressive loss of label which was accelerated by trypsin. Thrombin under these conditions prevented the loss of 32P-phosphate. These results are interpreted to indicate a thrombin-induced destruction of a phosphoprotein phosphatase. The protein kinase activity of phosphorylated platelet membranes using endogenous or exogenous protein substrates showed a significant reduction compared to non-phosphorylated membranes suggesting a deactivation of protein kinase by phosphorylation of platelet membranes. Neither thrombin nor trypsin caused a qualitative change in the membrane polypeptides accepting 32P-phosphate but resulted in quantitative alterations of their ability to become phosphorylated.


1989 ◽  
Vol 264 (24) ◽  
pp. 14549-14555 ◽  
Author(s):  
D Kübler ◽  
W Pyerin ◽  
O Bill ◽  
A Hotz ◽  
J Sonka ◽  
...  

1996 ◽  
Vol 191 (2) ◽  
pp. 281-282 ◽  
Author(s):  
J. Kanungo ◽  
B. Calhoun ◽  
Y. Takeda ◽  
J. A. Hardin ◽  
H. Rasmussen

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