Molecular interaction of anti-cancer ligands with human brain acetylcholinesterase

Author(s):  
Shazi Shakil
2012 ◽  
Vol 11 (2) ◽  
pp. 142-147 ◽  
Author(s):  
Shazi Shakil ◽  
Mohammad A. Kamal ◽  
Shams Tabrez ◽  
Adel M. Abuzenadah ◽  
Adeel G.A. Chaudhary ◽  
...  

2014 ◽  
Vol 13 (3) ◽  
pp. 487-490 ◽  
Author(s):  
Aftab Alam ◽  
Sibhghatulla Shaikh ◽  
Syed Ahmad ◽  
Mohammad Ansari ◽  
Shahnawaz Shakil ◽  
...  

2011 ◽  
Vol 10 (7) ◽  
pp. 845-848 ◽  
Author(s):  
Shazi Shakil ◽  
Rosina Khan ◽  
Shams Tabrez ◽  
Qamre Alam ◽  
Nasimudeen R. Jabir ◽  
...  

1996 ◽  
Vol 42 (1) ◽  
pp. 19-23 ◽  
Author(s):  
N Boschetti ◽  
U Brodbeck ◽  
S P Jensen ◽  
C Koch ◽  
B Nørgaard-Pedersen

Abstract Monoclonal antibodies (mAbs) were raised against a peptide of the 10 C-terminal amino acids of human brain acetylcholinesterase (AChE): H-Tyr-Ser-Lys-Gln-Asp-Arg-Cys-Ser-Asp-Leu-OH. Two positive clones (mAbs 190-1 and 190-2) were selected and tested for their ability to distinguish between mammalian brain and erythrocyte AChEs. In a solid-phase enzyme antigen immunoassay as well as by Western- and dot-blot analysis, both antibodies showed clear binding to AChE from human and bovine brain but not to AChE from erythrocytes. MAbs 190-1 and 190-2 reacted with neither AChE from electric eel nor butyrylcholinesterase from human serum. Both antibodies were used in a quantitative assay for AChE in amniotic fluids, where AChE activity could be found only in samples from open neural tube-defect pregnancies, but not in fluids from normal pregnancies or in artificially blood-contaminated samples.


2003 ◽  
Vol 989 (2) ◽  
pp. 147-151
Author(s):  
Xing-Mei Zhang ◽  
Qian Li ◽  
Yu-Sheng Shi ◽  
Jun-Hua Wu ◽  
Ning-Sheng Shao ◽  
...  

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