Estimation of binding constants for the substrate and activator of Rhodobacter sphaeroides adenosine 5′-diphosphate-glucose pyrophosphorylase using affinity capillary electrophoresis

Kaddis, John; Zurita, Cecilia; Morán, Julio; Borra, Margie T.; Polder, Nephi; Meyer, Christopher R.; Gomez, Frank A.

doi:10.1016/j.ab.2004.01.023

Cited by 15 publications

(9 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The apparent contradiction between binding affinity and the catalytic activity was also observed with the Rhodobacter sphaeroides AGPase mutant containing the R 22 A mutation (Kaddis et al, 2004) which bound ATP but not in the proper orientation for catalysis.…”

Section: Discussionmentioning

confidence: 79%

Catalytic implications of the higher plant ADP-glucose pyrophosphorylase large subunit

2007

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 79%

Catalytic implications of the higher plant ADP-glucose pyrophosphorylase large subunit

2007

View full text Add to dashboard Cite

“…The inconsistencies in the EOF and variations of electrophoretic mobility due to fluctuations in the voltage and current in a single run can also be a problem. A reliable way to minimize these factors is to use reference standards to obtain RMTRs 20–22, 24, 25, 55, 71–79 instead of mobility. The use of RMTR allows a voltage gradient to be used for accurate estimation of binding constants 62.…”

Section: Ce‐based Methodsmentioning

confidence: 99%

Use of CE for the determination of binding constants

2009

View full text Add to dashboard Cite

In the past two decades, CE has been used frequently for the measurement of apparent binding/association constants. CE has numerous advantages, including short analysis times, low sample consumption, simplicity of operation, etc. This review provides a fundamental introduction to binding theory and then summarizes recent applications and advances in the field of CE-based methods for the evaluation of molecular association. The time period for this survey is from 2002 (when our previous review was published) to the present.

show abstract

“…Kaddis et al recently determined binding constants for the activator fructose-6-phosphate (F6P) and substrate ATP to the recombinant wild-type (WT) Rhodobacter sphaeroides adenosine 5'-diphosphate-(ADP)-glucose pyrophosphorylase (ADPGlc PPase) using ACE [17]. In these studies, the capillary was initially injected with a plug of sample containing ADPGlc PPase and non-interacting standards.…”

Section: Protein-small Moleculementioning

confidence: 99%

Recent Developments in Affinity Capillary Electrophoresis: A Review

Zavaleta¹,

Chinchilla²,

Brown³

et al. 2006

CAC

View full text Add to dashboard Cite

Affinity capillary electrophoresis (ACE) is a versatile analytical technique that has been shown to be an efficient and accurate tool to probe non-covalent interactions and to determine binding and dissociation constants between receptors and ligands. ACE uses as its basis the change in migration time of a receptor upon binding to a ligand generally found in the electrophoresis buffer. Subsequent analysis using non-interacting standards realizes values for the binding constant. The technique has a number of advantages over other binding assay methods in that binding parameters can be obtained expeditiously, reproducibly, and with minimal sample quantity requirements and preparation. This review focuses on the literature describing the use of ACE from

show abstract

Estimation of binding constants for the substrate and activator of Rhodobacter sphaeroides adenosine 5′-diphosphate-glucose pyrophosphorylase using affinity capillary electrophoresis

Cited by 15 publications

References 29 publications

Catalytic implications of the higher plant ADP-glucose pyrophosphorylase large subunit

Catalytic implications of the higher plant ADP-glucose pyrophosphorylase large subunit

Use of CE for the determination of binding constants

Recent Developments in Affinity Capillary Electrophoresis: A Review

Contact Info

Product

Resources

About