Correction to The Kinase Activity of the Helicobacter pyloriAsp-tRNAAsn/Glu-tRNAGln Amidotransferase Is Sensitive to Distal Mutations in Its Putative Ammonia Tunnel

Biochemistry ◽  
2013 ◽  
Vol 52 (13) ◽  
pp. 2381-2381
Author(s):  
Liangjun Zhao ◽  
Sajeewa W. Dewage ◽  
Michael J. Bell ◽  
Keng-Ming Chang ◽  
Shirin Fatma ◽  
...  
Keyword(s):  
Kinase Activity ◽  
Ammonia Tunnel

scholarly journals The Kinase Activity of the Helicobacter pylori Asp-tRNAAsn/Glu-tRNAGln Amidotransferase Is Sensitive to Distal Mutations in Its Putative Ammonia Tunnel

Biochemistry ◽  
2011 ◽  
Vol 51 (1) ◽  
pp. 273-285 ◽  
Author(s):  
Liangjun Zhao ◽  
Sajeewa W. Dewage ◽  
Michael J. Bell ◽  
Keng-Ming Chang ◽  
Shirin Fatma ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Kinase Activity ◽  
Ammonia Tunnel

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.

Sign in / Sign up

Export Citation Format

Share Document