Corrections - Binding Kinetics of Methyl α-D-Mannopyranoside to Concanavalin A: Temperature-Jump Relaxation Study with 4-Methylumbelliferyl α-D-Mannopyranoside as a Fluorescence Indicator Ligand

Biochemistry ◽  
1982 ◽  
Vol 21 (12) ◽  
pp. 3036-3036
Author(s):  
Robert Clegg ◽  
Frank Loontiens ◽  
Anita Van Landschoot ◽  
Thomas Jovin
Keyword(s):  
Concanavalin A ◽  
Temperature Jump ◽  
Binding Kinetics ◽  
Relaxation Study ◽  
Kinetics Of

Kinetics of the equilibration of 3-hydroxyphthalide and o-formylbenzoic acid. Hemiacetal breakdown with a carboxylic acid leaving group

1986 ◽  
Vol 64 (6) ◽  
pp. 1196-1200 ◽  
Author(s):  
Robert A. McClelland ◽  
Poule E. Sørensen
Keyword(s):  
Carboxylic Acid ◽  
Ring Opening ◽  
Temperature Jump ◽  
Acid Catalyst ◽  
Concerted Mechanism ◽  
Leaving Group ◽  
Relaxation Study ◽  
Acid Catalyzed ◽  
Kinetics Of ◽  
Conjugate Base

A temperature-jump relaxation study is reported for the equilibration: 3-hydroxyphthalide (SH) [Formula: see text]o-formylbenzoate (R−) [Formula: see text]o-formylbenzoic acid (RH). A kinetic analysis is carried out in which SH and R− interconvert with catalysis in the ring opening direction by water and by added general bases. Excellent Brønsted plots based upon a series of oxyacid buffer catalysts are obtained. These have slopes β for the base-catalyzed ring opening of 0.81 and α for the reverse acid-catalyzed ring closing of 0.19. A mechanism where S−, the conjugate base of SH, is a discrete intermediate can be ruled out on the basis of the Brønsted values and the magnitudes of the rate constants. The lifetime of S− is estimated to lie in the range 10−11–10−15 s. Two mechanisms can be proposed. A fully concerted mechanism "enforced" by lifetimes less than 10−13 s involves direct interconversion of SH and R− with no intermediate. A preassociated mechanism "enforced" by lifetimes in the 10−11–10−12 s range requires, in the ring closing direction, that an acid catalyst be hydrogen bonded to the carbonyl in R−.

Binding of 4-methylumbelliferyl α-D-mannopyranoside to dimeric concanavalin A: fluorescence temperature-jump relaxation study

Biochemistry ◽  
1977 ◽  
Vol 16 (2) ◽  
pp. 167-175 ◽  
Author(s):  
Robert M. Clegg ◽  
Frank G. Loontiens ◽  
Thomas M. Jovin
Keyword(s):  
Concanavalin A ◽  
Temperature Jump ◽  
Relaxation Study

scholarly journals Binding Kinetics of 4-Methylumbelliferyl alpha-Mannobioside to Concanavalin A by Fluorescence Stopped-Flow Measurements

1980 ◽  
Vol 103 (2) ◽  
pp. 313-321 ◽  
Author(s):  
Anita LANDSCHOOT ◽  
Frank G. LOONTIENS ◽  
Robert M. CLEGG ◽  
Thomas M. JOVIN
Keyword(s):  
Concanavalin A ◽  
Binding Kinetics ◽  
Stopped Flow ◽  
Flow Measurements ◽  
Kinetics Of

scholarly journals Binding of 4-Methylumbelliferyl alpha-d-Mannopyranoside to Tetrameric Concanavalin A. Fluorescence Temperature-Jump Relaxation Study

1977 ◽  
Vol 78 (2) ◽  
pp. 465-469 ◽  
Author(s):  
Frank G. LOONTIENS ◽  
Anita LANDSCHOOT ◽  
Robert M. CLEGG ◽  
Thomas M. JOVIN
Keyword(s):  
Concanavalin A ◽  
Temperature Jump ◽  
Relaxation Study

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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