Anticholine esterase activity of phosphonium bis-zwitterions based on 2-cyanoacrylates

1999 ◽  
Vol 48 (11) ◽  
pp. 2167-2169 ◽  
Author(s):  
Yu. G. Zhukovskii ◽  
L. P. Kuznetsova ◽  
E. E. Sochilina ◽  
Y. Yu. Bykovskaya ◽  
T. O. Krylova ◽  
...  

ChemInform ◽  
2010 ◽  
Vol 31 (13) ◽  
pp. no-no
Author(s):  
Yu. G. Zhukovskii ◽  
L. P. Kuznetsova ◽  
E. E. Sochilina ◽  
E. Yu. Bykovskaya ◽  
T. O. Krylova ◽  
...  


1991 ◽  
Vol 25 (4) ◽  
pp. 258-260
Author(s):  
V. B. Sokolov ◽  
Yu. Ya. Ivanov ◽  
T. A. Epishina ◽  
I. V. Martynov


1967 ◽  
Vol 17 (03/04) ◽  
pp. 321-334 ◽  
Author(s):  
J. P Soulier ◽  
Odette Prou-Wartelle ◽  
Liliane Hallé ◽  

SummaryThe preparation of thrombin-coagulase is described. The properties of thrombin-coagulase are compared with those of biothrombin: kinetics, thermostability, adsorption, chromatography, esterase activity, clotting activity, action on platelets and on factors V and VIII, susceptibility to inhibitors.Biothrombin and thrombin-coagulase are closely related but distinct. Both apparently derive from prothrombin. Prothrombin and coagulase combine to form a complex: thrombin-coagulase wherein both factors are necessary for its activity. Possible explanations for the difference between thrombin-coagulase and biothrombin are proposed.



1966 ◽  
Vol 16 (01/02) ◽  
pp. 018-031 ◽  
Author(s):  
S Sherry ◽  
Norma Alkjaersig ◽  
A. P Fletcher

SummaryComparative studies have been made of the esterase activity of plasmin and the streptokinase-activator of plasminogen on a variety of substituted arginine and lysine esters. Human plasmin preparations derived by different methods of activation (spontaneous in glycerol, trypsin, streptokinase (SK) and urokinase) are similar in their esterase activity; this suggests that the molecular structure required for such esterase activity is similar for all of these human plasmins. Bovine plasmin, on the other hand, differs from human plasmin in its activity on several of the substrates studied (e.g., the methyl esters of benzoyl arginine and tosyl, acetyl and carbobenzoxy lysine), a finding which supports the view that molecular differences exist between the two animal plasmins. The streptokinase-activator hydrolyzes both arginine and lysine esters but the ratios of hydrolytic activity are distinct from those of plasmin and of other activators of plasminogen. The use of benzoyl arginine methyl ester as a substrate for the measurement of the esterase activity of the streptokinase-activator is described.



1989 ◽  
Vol 264 (22) ◽  
pp. 13289-13297
Author(s):  
S Chwetzoff ◽  
S Tsunasawa ◽  
F Sakiyama ◽  
A Ménez


1950 ◽  
Vol 182 (2) ◽  
pp. 577-584
Author(s):  
John E. Snoke ◽  
Hans. Neurath


1995 ◽  
Vol 36 (11) ◽  
pp. 2303-2310
Author(s):  
I Ishii ◽  
R Onozaki ◽  
E Takahashi ◽  
S Takahashi ◽  
N Fujio ◽  
...  


1972 ◽  
Vol 247 (4) ◽  
pp. 1265-1271
Author(s):  
J. Tyson Tildon ◽  
James W. Ogilvie
Keyword(s):  


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