Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus

Biochemistry ◽  
1995 ◽  
Vol 34 (40) ◽  
pp. 12926-12931 ◽  
Author(s):  
Antonius C. F. Gorren ◽  
Pierre Moenne-Loccoz ◽  
Gabriele Backes ◽  
Simon de Vries ◽  
Joann Sanders-Loehr ◽  
...  
FEBS Letters ◽  
1993 ◽  
Vol 333 (1-2) ◽  
pp. 188-192 ◽  
Author(s):  
Jozef Van Beeumen ◽  
Gonzalez Van Driessche ◽  
Fienke Huitema ◽  
J.A. Duine ◽  
Gerard W. Canters

1991 ◽  
Vol 202 (3) ◽  
pp. 1011-1012
Author(s):  
Marcellus UBBINK ◽  
Mario A. G. KLEEF ◽  
Dirk-Jan KLEINJAN ◽  
Carla W. G. HOITINK ◽  
Fienke HUITEMA ◽  
...  

1991 ◽  
Vol 202 (3) ◽  
pp. 1003-1012 ◽  
Author(s):  
Marcellus UBBINK ◽  
Mario A. G. KLEEF ◽  
Dirk-Jan KLEINJAN ◽  
Carla W. G. HOITINK ◽  
Fienke HUITEMA ◽  
...  

1996 ◽  
Vol 76 (01) ◽  
pp. 005-008 ◽  
Author(s):  
Jean Claude Lormeau ◽  
Jean Pascal Herault ◽  
Jean Marc Herbert

SummaryWe examined the effect of the synthetic pentasaccharide representing the minimal binding site of heparin to antithrombin on the antithrombin-mediated inactivation of factor Vila bound to tissue factor. This effect was compared to the effect of unfractionated heparin. Using purified recombinant human coagulation factors and either a clotting or an amidolytic assay for the determination of the residual activity of factor Vila, we showed that the pentasaccharide was an efficient antithrombin-dependent inhibitor of the coagulant activity of tissue factor-factor Vila complex. In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 ± 10,500 min-1 and 112,000 ± 12,000 min-1 (mean ± s.e.m., n = 3)


Sign in / Sign up

Export Citation Format

Share Document