Journal ArticleDOI
Equivalence of certain models in protein ligand equilibria and the possibility of distinguishing between them.
Magar E. Magar,Robert F. Steiner +1 more
TLDR
Methods have been developed for analyzing the binding of ligand by a protein exhibiting allosteric properties and the relationship to existing theoretical models has been discussed.About:
This article is published in Journal of Theoretical Biology.The article was published on 1971-09-01. It has received 11 citations till now. The article focuses on the topics: Protein ligand & Allosteric regulation.read more
Citations
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Catalytic and regulatory site composition of yeast AMP deaminase by comparative binding and rate studies. Resolution of the cooperative mechanism.
D J Merkler,Vern L. Schramm +1 more
TL;DR: The traditional cooperative binding models of allosteric regulation do not apply to yeast AMP deaminase, which regulates catalytic activity by kinetic control of product formation, and no cooperativity is observed in the binding of any of the regulator ligands and ATP binding and kinetic activation by ATP is independent of substrate analog concentration.
Journal ArticleDOI
Hemocyanin from the Australian freshwater crayfish Cherax destructor. Oxygen binding studies of major components.
P D Jeffrey,G B Treacy +1 more
TL;DR: Oxygen binding curves have been obtained for unfractionated hemocyanin from Cherax destructor and it major components, the 25S and 17S forms, and there was no evidence of concentration dependence of the binding curves in the range 0.6-6 mg/mL, a finding which excludes a dynamic equilibrium between polymeric forms of different oxygen affinity as a source of the cooperative binding.
Journal ArticleDOI
Alternative interpretation of unusual scatchard plots: contribution of interactions and heterogeneity
Marco V. José,Carlos Larralde +1 more
TL;DR: In this paper, it was shown that positive and negative site-site interactions in homogeneous and heterogeneous macromolecules result in varied binding isotherms, some with quite unusual shapes.
Journal ArticleDOI
Kinetics of adenosine monophosphate nucleosidase inactivation by phosphate and protection by substrate and allosteric activator.
Vern L. Schramm,F A Fullin +1 more
TL;DR: The results suggest that inactivation occurs after two or more of the six allosteric sites for Pi have been filled, and is consistent with a mechanism in which a ternary complex of enzyme is formed.
Journal ArticleDOI
The binding of lipid to the lipid-free adenosine triphosphatase protein of sarcoplasmic reticulum.
TL;DR: Dinitrophenylated dipalmitoyl phosphatidylethanolamine and its lyso derivative have been shown to bind to the lipid-free ATPase protein derived from the sarcoplasmic reticulum.
References
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Journal ArticleDOI
The Attractions of Proteins for Small Molecules and Ions
TL;DR: The number and variety of known compounrjs between proteins and small molecules are increasing rapidly and make a fascinating story as discussed by the authors, and there are many compounds of serum albumin, which was used during the war by many chemists, most of whom found at least one 6ew compound.
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On the Nature of Allosteric Transitions: A Plausible Model
TL;DR: "It is certain that all bodies whatsoever, though they have no sense, yet they have perception, and whether the body be alterant or alterec, evermore a perception precedeth operation; for else all bodies would be like one to another."
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On the nature of allosteric transitions: implications of non-exclusive ligand binding.
TL;DR: The non-exclusive binding of one or more of the ligands, such as the substrate, inhibitor or activator of a regulatory enzyme, is expected to introduce limits on the extent to which the equilibrium between the conformational states of an allosteric protein may be shifted in their presence.
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Treatment of Enzyme Kinetic Data II. THE MULTISITE CASE: COMPARISON OF ALLOSTERIC MODELS AND A POSSIBLE NEW MECHANISM
TL;DR: Various methods of plotting allosteric data are discussed with the conclusion that plots of initial velocity divided by substrate concentration (v/S) versus the initial velocity are most convenient.
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Models for Cooperative Effects in Proteins Containing Subunits EFFECTS OF TWO INTERACTING LIGANDS
TL;DR: The results indicate that the sequential model is capable of explaining a wide variety of kinetic data involving activators, inhibitors, and cooperative effects and is more general but more complex than the symmetry model of Monod, Wyman, and Changeux.