Configuration of the methyl ester of dimethylphosphinic acid

1970 ◽  
Vol 19 (8) ◽  
pp. 1629-1633
Author(s):  
O. A. Raevskii ◽  
R. R. Shagidullin ◽  
I. D. Morozova ◽  
L. E. Petrova ◽  
F. G. Khalitov
Keyword(s):  
Methyl Ester ◽  
Dimethylphosphinic Acid

The IR spectra and structure of the methyl ester of dimethylphosphinic acid

1973 ◽  
Vol 18 (3) ◽  
pp. 364-366
Author(s):  
A. B. Remizov ◽  
�. G. Yarkova ◽  
I. Ya. Kuramshin ◽  
A. A. Muratova
Keyword(s):  
Methyl Ester ◽  
Ir Spectra ◽  
Dimethylphosphinic Acid

The Effect of Some Synthetic Arginyl and Lysyl Compounds on Clotting and Fibrinolysis

1972 ◽  
Vol 28 (02) ◽  
pp. 289-298 ◽  
Author(s):  
M. J Weinstein ◽  
R. F Doolittle
Keyword(s):  
Methyl Ester ◽  
Thrombin Activation

SummaryThe effects of a number of synthetic arginyl- and lysyl-compounds on clotting and fibrinolysis have been studied. The lysyl derivatives had no significant effect on the clotting of recalcified plasma or recalcified euglobulin preparations, but tosyllysine (TL) and tosyllysine methyl ester (TLME) were very effective inhibitors of fibrinolysis. Certain arginyl-peptides (in particular, tosylarginylsarcosine methyl ester) were very effective at delaying clotting in these systems. These same substances gave rise to an exaggerated thrombin production, however, evidently by interfering with the natural thrombin activation of plasma antithrombin(s).

Activity of Plasmin and Streptokinase-Activator on Substituted Arginine and Lysine Esters

1966 ◽  
Vol 16 (01/02) ◽  
pp. 018-031 ◽  
Author(s):  
S Sherry ◽  
Norma Alkjaersig ◽  
A. P Fletcher
Keyword(s):  
Molecular Structure ◽  
Methyl Ester ◽  
Comparative Studies ◽  
Esterase Activity ◽  
Methyl Esters ◽  
Hydrolytic Activity ◽  
The Other ◽  
Other Hand

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.

Photoinduced N-Demethylation of Rufloxacin and its Methyl Ester Under Aerobic Conditions¶

2002 ◽  
Vol 76 (3) ◽  
pp. 252 ◽  
Author(s):  
Alessandra Belvedere ◽  
Francisco Boscá ◽  
M. Consuelo Cuquerella ◽  
Guido de Guidi ◽  
Miguel A. Miranda
Keyword(s):  
Methyl Ester ◽  
Aerobic Conditions
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