scholarly journals Membrane binding kinetics of factor VIII indicate a complex binding process.

1993 ◽  
Vol 268 (12) ◽  
pp. 8815-8824
Author(s):  
C. Bardelle ◽  
B. Furie ◽  
B.C. Furie ◽  
G.E. Gilbert
Keyword(s):  
Factor Viii ◽  
Membrane Binding ◽  
Binding Kinetics ◽  
Binding Process ◽  
Kinetics Of

scholarly journals Membrane Binding Kinetics of Endophilin N-BAR Domain

2012 ◽  
Vol 102 (3) ◽  
pp. 97a-98a
Author(s):  
Wan-Ting Hsieh ◽  
Tobias Baumgart
Keyword(s):  
Membrane Binding ◽  
Binding Kinetics ◽  
Bar Domain ◽  
Kinetics Of

scholarly journals Comparison of the membrane binding kinetics of bovine prothrombin and its fragment 1.

1993 ◽  
Vol 268 (31) ◽  
pp. 22984-22991
Author(s):  
K.H. Pearce ◽  
M Hof ◽  
B.R. Lentz ◽  
N.L. Thompson
Keyword(s):  
Membrane Binding ◽  
Binding Kinetics ◽  
Kinetics Of

Membrane Binding Kinetics of Protein Kinase C βII Mediated by the C2 Domain†

Biochemistry ◽  
2001 ◽  
Vol 40 (44) ◽  
pp. 13216-13229 ◽  
Author(s):  
Eric A. Nalefski ◽  
Alexandra C. Newton
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Membrane Binding ◽  
Binding Kinetics ◽  
C2 Domain ◽  
Kinase C ◽  
Kinetics Of

The membrane binding kinetics of full-length PKCα is determined by membrane lipid composition

2012 ◽  
Vol 1821 (11) ◽  
pp. 1434-1442 ◽  
Author(s):  
Ángel Pérez-Lara ◽  
Antonio L. Egea-Jiménez ◽  
Alessio Ausili ◽  
Senena Corbalán-García ◽  
Juan C. Gómez-Fernández
Keyword(s):  
Lipid Composition ◽  
Membrane Binding ◽  
Membrane Lipid ◽  
Full Length ◽  
Binding Kinetics ◽  
Membrane Lipid Composition ◽  
Kinetics Of

Acquired Haemophilia: Functional Study of Antibodies to Factor VIII

1981 ◽  
Vol 45 (03) ◽  
pp. 285-289 ◽  
Author(s):  
J P Allain ◽  
A Gaillandre ◽  
D Frommel
Keyword(s):  
Factor Viii ◽  
Functional Study ◽  
Factor Viii Inhibitor ◽  
Acquired Haemophilia ◽  
Viii Inhibitor ◽  
Kinetics Of ◽  
Antibody Function ◽  
Native Plasma

SummaryFactor VIII complex and its interaction with antibodies to factor VIII have been studied in 17 non-haemophilic patients with factor VIII inhibitor. Low VIII:C and high VIIIR.Ag levels were found in all patients. VIII:WF levels were 50% of those of VTIIRrAg, possibly related to an increase of poorly aggregated and electrophoretically fast moving VIIIR:Ag oligomers.Antibody function has been characterized by kinetics of VIII :C inactivation, saturability by normal plasma and the slope of the affinity curve. Two major patterns were observed:1) Antibodies from 6 patients behaved similarly to those from haemophiliacs by showing second order inhibition kinetics, easy saturability and steep affinity slope (> 1).2) Antibodies from other patients, usually with lower titres, inactivated VIII :C according to complex order kinetics, were not saturable, and had a less steep affinity slope (< 0.7). In native plasma, or after mixing with factor VIII concentrate, antibodies of the second group did not form immune complexes with the whole factor VIII molecular complex. However, dissociation procedures did release some antibodies from apparently low molecular weight complexes formed in vivo or in vitro. For appropriate management of non-haemophilic patients with factor VIII inhibitor, it is important to determine the functional properties of their antibodies to factor VIII.

Binding kinetics of fluorescent bisphosphonates as a tool for monitoring bone dynamics in vivo

2013 ◽  
Author(s):  
Robert Tower ◽  
Graeme Campbell ◽  
Marc Muller ◽  
Olga Will ◽  
Frederieka Grundmann ◽  
...  
Keyword(s):  
Binding Kinetics ◽  
Kinetics Of ◽  
Bone Dynamics

Influence of Brain Gangliosides on the Formation and Properties of Supported Lipid Bilayers for Binding Kinetics Studies

2018 ◽  
Author(s):  
Luke Jordan ◽  
Nathan Wittenberg
Keyword(s):  
Lipid Bilayers ◽  
Binding Kinetics ◽  
Supported Lipid Bilayers ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Supported Lipid Bilayer ◽  
Head Groups ◽  
Lipid Diffusion ◽  
Kinetics Of ◽  
Brain Gangliosides

This is a comprehensive study of the effects of the four major brain gangliosides (GM1, GD1b, GD1a, and GT1b) on the adsorption and rupture of phospholipid vesicles on SiO2 surfaces for the formation of supported lipid bilayer (SLB) membranes. Using quartz crystal microbalance with dissipation monitoring (QCM-D) we show that gangliosides GD1a and GT1b significantly slow the SLB formation process, whereas GM1 and GD1b have smaller effects. This is likely due to the net ganglioside charge as well as the positions of acidic sugar groups on ganglioside glycan head groups. Data is included that shows calcium can accelerate the formation of ganglioside-rich SLBs. Using fluorescence recovery after photobleaching (FRAP) we also show that the presence of gangliosides significantly reduces lipid diffusion coefficients in SLBs in a concentration-dependent manner. Finally, using QCM-D and GD1a-rich SLB membranes we measure the binding kinetics of an anti-GD1a antibody that has similarities to a monoclonal antibody that is a hallmark of a variant of Guillain-Barre syndrome.

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