Water−Ethylene Glycol Alkyltrimethylammonium Bromide Micellar Solutions as Reaction Media:  Study of Spontaneous Hydrolysis of Phenyl Chloroformate

Langmuir ◽  
2003 ◽  
Vol 19 (18) ◽  
pp. 7206-7213 ◽  
Author(s):  
Amalia Rodríguez ◽  
María del Mar Graciani ◽  
María Muñoz ◽  
María Luisa Moyá
Langmuir ◽  
2003 ◽  
Vol 19 (21) ◽  
pp. 8685-8691 ◽  
Author(s):  
María del Mar Graciani ◽  
Amalia Rodríguez ◽  
María Muñoz ◽  
María Luisa Moyá

2009 ◽  
Vol 113 (22) ◽  
pp. 7767-7779 ◽  
Author(s):  
Amalia Rodríguez ◽  
María del Mar Graciani ◽  
Felipe Cordobés ◽  
María Luisa Moyá

2018 ◽  
Vol 100 ◽  
pp. 18-24 ◽  
Author(s):  
Dmitry V. Orekhov ◽  
Oleg A. Kazantsev ◽  
Alexey P. Sivokhin ◽  
Maria V. Savinova

1959 ◽  
Vol 37 (1) ◽  
pp. 1361-1366 ◽  
Author(s):  
Ricardo H. Landaburu ◽  
Walter H. Seegers

Purified thrombin-C loses its clotting power upon acetylation. The thrombin-E which is produced during the acetylation has approximately twice the proteolytic activity as the original thrombin-C. Evidently amino groups are not necessary to have thrombin-E activity, but if o-acyl groups are also produced the enzyme does not hydrolyze p-toluenesulphonylarginine methyl ester (TAMe). The activity can be recovered by spontaneous hydrolysis of the o-acyl groups at pH 8.5. Thrombin-E does not activate fibrinogen, but does lyse fibrin. The optimum pH with TAMe as substrate is 8.8. It may be that thrombin-C is a dimer of the basic structure in thrombin-E.


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