Plasma esterase activity in patients with aspirin-sensitive asthma or urticaria

1987 ◽  
Vol 33 (4) ◽  
pp. 387-390 ◽  
Author(s):  
F. M. Williams ◽  
S. I. Asad ◽  
M. H. Lessof ◽  
M. D. Rawlins
Pharmacology ◽  
1979 ◽  
Vol 18 (6) ◽  
pp. 294-298 ◽  
Author(s):  
R. Calvo ◽  
R. Carlos ◽  
S. Erill

1964 ◽  
Vol 42 (12) ◽  
pp. 1711-1715 ◽  
Author(s):  
D. G. Baker ◽  
R. Ghys ◽  
D. Coles ◽  
S. Christie

Qualitative changes occurred in the spectrum of plasma esterase activity with increasing age. The trend was toward a decrease in the number of specific proteins having esterase activity. Acclimation to cold did not accelerate the onset of this trend. In the plasma esterase activity during acclimation to cold, there were no changes which would suggest accelerated aging.


Endocrinology ◽  
1984 ◽  
Vol 115 (6) ◽  
pp. 2406-2417 ◽  
Author(s):  
SUSAN S. KADNER ◽  
JOSEPH KATZ ◽  
BRETT A. BERLINER ◽  
MORTIMER LEVITZ ◽  
THOMAS H. FINLAY

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

Sign in / Sign up

Export Citation Format

Share Document