Time-gated luminescence assay using nonmetal probes for determination of protein kinase activity-based disease markers

2012 ◽  
Vol 422 (2) ◽  
pp. 79-88 ◽  
Author(s):  
Marje Kasari ◽  
Peeter Padrik ◽  
Angela Vaasa ◽  
Kristi Saar ◽  
Krista Leppik ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Disease Markers ◽  
Luminescence Assay

scholarly journals Determination of Human Myosin III as a Motor Protein Having a Protein Kinase Activity

2003 ◽  
Vol 278 (24) ◽  
pp. 21352-21360 ◽  
Author(s):  
Shigeru Komaba ◽  
Akira Inoue ◽  
Shinsaku Maruta ◽  
Hiroshi Hosoya ◽  
Mitsuo Ikebe
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Motor Protein ◽  
Protein Kinase Activity

Determination of cyclic nucleotide-responsive protein kinase activity by quantitative fast atom bombardment mass spectrometry

1992 ◽  
Vol 20 (2) ◽  
pp. 152S-152S
Author(s):  
ANDREA M. EVANS ◽  
FRANK M. HARRIS ◽  
TERENCE J. WALTON ◽  
A. GARETH BRENTON ◽  
JAMES I. LANGRIDGE ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Kinase ◽  
Cyclic Nucleotide ◽  
Fast Atom Bombardment ◽  
Kinase Activity ◽  
Protein Kinase Activity

Effect of Thrombin on Phosphorylation of Platelet Membrane Proteins

1976 ◽  
Vol 35 (03) ◽  
pp. 635-642 ◽  
Author(s):  
M Steiner
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Qualitative Change ◽  
Protein Kinase Activity ◽  
Protein Substrates ◽  
Phosphoprotein Phosphatase ◽  
Progressive Loss ◽  
Platelet Membranes ◽  
Endogenous Protein ◽  
Considerable Loss

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.

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