Rare Earth Ion Mediated Fluorescence Accumulation on a Single Microbead: An Ultrasensitive Strategy for the Detection of Protein Kinase Activity at the Single-Cell Level

2015 ◽  
Vol 54 (50) ◽  
pp. 15186-15190 ◽  
Author(s):  
Xiaobo Zhang ◽  
Chenghui Liu ◽  
Honghong Wang ◽  
Hui Wang ◽  
Zhengping Li
Keyword(s):  
Rare Earth ◽  
Protein Kinase ◽  
Single Cell ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Single Cell Level ◽  
Cell Level ◽  
Rare Earth Ion

Label-free and ultrasensitive detection of polynucleotide kinase activity at the single-cell level

2018 ◽  
Vol 54 (13) ◽  
pp. 1583-1586 ◽  
Author(s):  
Meng Liu ◽  
Fei Ma ◽  
Qianyi Zhang ◽  
Chun-yang Zhang
Keyword(s):  
Single Cell ◽  
Kinase Activity ◽  
Fluorescence Method ◽  
Kinase Assay ◽  
Ultrasensitive Detection ◽  
Single Cell Level ◽  
Label Free ◽  
Cell Level ◽  
Polynucleotide Kinase

We develop a label-free fluorescence method for the polynucleotide kinase assay at the single-cell level based on phosphorylation-triggered isothermal exponential amplification.

A modified exponential amplification reaction (EXPAR) with an improved signal-to-noise ratio for ultrasensitive detection of polynucleotide kinase

2019 ◽  
Vol 55 (53) ◽  
pp. 7611-7614 ◽  
Author(s):  
Yu-Peng Zhang ◽  
Yun-Xi Cui ◽  
Xiao-Yu Li ◽  
Yi-Chen Du ◽  
An-Na Tang ◽  
...  
Keyword(s):  
Single Cell ◽  
Kinase Activity ◽  
Signal To Noise Ratio ◽  
Ultrasensitive Detection ◽  
Single Cell Level ◽  
Signal To Noise ◽  
Cell Level ◽  
Polynucleotide Kinase ◽  
Noise Ratio ◽  
Amplification Reaction

We reported a modified exponential amplification reaction strategy and applied it to design an ultrasensitive biosensor for the detection of endogenous polynucleotide kinase activity at single-cell level.

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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