W-Band ENDOR Investigation of the Manganese-Binding Site of Concanavalin A:  Determination of Proton Hyperfine Couplings and Their Signs

2000 ◽  
Vol 122 (14) ◽  
pp. 3488-3494 ◽  
Author(s):  
Palanichamy Manikandan ◽  
Raanan Carmieli ◽  
Tania Shane ◽  
A. Joseph Kalb (Gilbo ◽  
Daniella Goldfarb
Keyword(s):  
Binding Site ◽  
Concanavalin A ◽  
W Band ◽  
Hyperfine Couplings ◽  
Manganese Binding Site

Antithrombin-mediated Inhibition of Factor Vlla-Tissue Factor Complex by the Synthetic Pentasaccharide Representing the Heparin Binding Site to Antithrombin

1996 ◽  
Vol 76 (01) ◽  
pp. 005-008 ◽  
Author(s):  
Jean Claude Lormeau ◽  
Jean Pascal Herault ◽  
Jean Marc Herbert
Keyword(s):  
Binding Site ◽  
Tissue Factor ◽  
Residual Activity ◽  
Coagulation Factors ◽  
Heparin Binding ◽  
Experimental Conditions ◽  
First Order ◽  
Heparin Binding Site ◽  
Coagulant Activity

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)

Characterization of Glycoprotein Fraction from Carp Pituitaries Isolated Using Concanavalin A as the Affinity Ligand

1998 ◽  
Vol 63 (3) ◽  
pp. 434-440 ◽  
Author(s):  
Irena Hulová ◽  
Jana Barthová ◽  
Helena Ryšlavá ◽  
Václav Kašička
Keyword(s):  
Concanavalin A ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Gel Chromatography ◽  
Affinity Ligand ◽  
Sds Page ◽  
Terminal Amino ◽  
Α And Β Subunits

Glycoproteins that have affinity to Concanavalin A were isolated from the acetone-dried pituitaries of common carp (Cyprinus carpio L.). Two fractions of glycoproteins were separated using gel chromatography on Superdex 75HR. The fraction with lower molecular weight (30 000) corresponding to the carp gonadotropin cGtH II was composed of two subunits as determined using SDS-PAGE. This protein fraction was further divided into four components using reversed-phase HPLC. Two fractions were pure α and β subunits of cGtH II as follows from immunodetection and from determination of N-terminal amino acid sequences. The other two were a mixture of α and β subunits as was also revealed by N-terminal analysis. Capillary electrophoresis was also used for characterization of isolated glycoproteins.

Determination of the binding site size of hexaammineruthenium(iii) inside monolayers of DNA on gold

The Analyst ◽  
2021 ◽  
Author(s):  
Alireza Abi ◽  
Afsaneh Safavi
Keyword(s):  
Metal Complex ◽  
Binding Site ◽  
Dna Strands

Hexaammineruthenium(iii) metal complex can bind to surface-tethered DNA strands in excess of what is required for the compensation of the DNA charges.

scholarly journals Crystallographic determination of the heme orientation and location of the cyanide binding site in yeast cytochrome c peroxidase.

1978 ◽  
Vol 253 (10) ◽  
pp. 3730-3735
Author(s):  
T.L. Poulos ◽  
S.T. Freer ◽  
R.A. Alden ◽  
N.H. Xuong ◽  
S.L. Edwards ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Binding Site ◽  
Cytochrome C Peroxidase ◽  
Cyanide Binding
Sign in / Sign up

Export Citation Format

Share Document