Stability Studies on Maize Leaf Phosphoenolpyruvate Carboxylase: The Effect of Salts

Jensen, Wayne A.; Armstrong, J. M.; Giorgio, Joseph; Hearn, Milton Thomas William

doi:10.1021/bi00002a011

Cited by 27 publications

(13 citation statements)

References 39 publications

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“…The activation parameters, in the presence of sodium phosphate, NaCl and (NH 4 + ) 2 SO 4 , point out the role played by ionic and hydrophobic interactions in the stabilization process of OCT and closely follow the Hofmeister series of anions (phosphate > SO 4 = > Cl − ). A similar trend in stabilization process has been noted by Damodoran [48] and Jensen et al [49]. The effects of ornithine could be due to conformational changes (as it can be seen by CD spectrum).…”

Section: Discussionsupporting

confidence: 83%

Stabilization effects of kosmotrope systems on ornithine carbamoyltransferase

Barreca

Bellocco

Galli

et al. 2009

International Journal of Biological Macromolecules

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Section: Discussionsupporting

confidence: 83%

Stabilization effects of kosmotrope systems on ornithine carbamoyltransferase

Barreca

Bellocco

Galli

et al. 2009

International Journal of Biological Macromolecules

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“…It is known to be a compatible solute (27,28). It enhances protein-nucleic acid interaction and stabilizes proteins from temperature inactivation (12,29). Several osmolytes play another important role in some organisms; that is, they counteract the effect of urea on protein structure.…”

Section: Discussionmentioning

confidence: 99%

Glutamate Counteracts the Denaturing Effect of Urea through Its Effect on the Denatured State

Mandal

Samaddar

Banerjee

et al. 2003

Journal of Biological Chemistry

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The urea induced equilibrium denaturation behavior of glutaminyl-tRNA synthetase from Escherichia coli (GlnRS) in 0.25 M potassium L-glutamate, a naturally occurring osmolyte in E. coli, has been studied. Both the native to molten globule and molten globule to unfolded state transitions are shifted significantly toward higher urea concentrations in the presence of L-glutamate, suggesting that L-glutamate has the ability to counteract the denaturing effect of urea. D-Glutamate has a similar effect on the equilibrium denaturation of glutaminyltRNA synthetase, indicating that the effect of L-glutamate may not be due to substrate-like binding to the native state. The activation energy of unfolding is not significantly affected in the presence of 0.25 M potassium L-glutamate, indicating that the native state is not preferentially stabilized by the osmolyte. Dramatic increase of coefficient of urea concentration dependence (m) values of both the transitions in the presence of glutamate suggests destabilization and increased solvent exposure of the denatured states. Four other osmolytes, sorbitol, trimethylamine oxide, inositol, and triethylene glycol, show either a modest effect or no effect on native to molten globule transition of glutaminyl-tRNA synthetase. However, glycine betaine significantly shifts the transition to higher urea concentrations. The effect of these osmolytes on other proteins is mixed. For example, glycine betaine counteracts urea denaturation of tubulin but promotes denaturation of S228N -repressor and carbonic anhydrase. Osmolyte counteraction of urea denaturation depends on osmolyte-protein pair.Folding of a polypeptide chain into a precise three-dimensional structure has been a subject of intense study over the past several decades (1, 2). Despite much progress, a complete understanding still eludes us. Much attention is now devoted to protein folding in vivo, where the cellular environment profoundly influences folding (3, 4). This has led to the discovery of the chaperones. Another aspect of in vivo environments that differ significantly from in vitro environments normally used for protein folding studies is the presence of osmolytes. Osmolytes are small molecules that accumulate inside the cell at relatively high concentrations and protect the intracellular proteins against environmental stress. Thus, they play a crucial role in protein stabilization.Although some efforts have been directed toward understanding the effects of osmolytes on protein stability, little is known about their effect on folding intermediates and partially unfolded states of proteins. Partially unfolded states are not only of crucial importance in understanding the folding processes but may play a crucial role in many diseases that involve extracellular protein aggregation and amyloid fibril formation, such as Alzheimer's disease and Scrapie (5, 6). Similar intracellular protein aggregates (Lewy bodies) are also known to play an important role in other neurodegenerative diseases, such as Parkinson's disease (7). Ver...

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“…Proteins have been known to have specific ion binding sites Pace & Grimsley, 1988!. Some ions bind to proteins at very low concentrations and affect their stability~Makhatadze et al, 1998!, while other salts affect the stability in a general manner without having any specificity toward proteins~von Hippel & Schleich, 1969;Busby et al, 1981;Arakawa et al, 1990b;Bonnette et al, 1994;Jensen et al, 1995!. The differential stability provided by salts of different combinations indicates the contribution of both the cations and anions for providing stability to the protein to an extent depending on their position in the Hofmeister series~Hofmeister, 1888; Baldwin, 1996!. In salt systems the effect of an individual ion has been found to be essentially additive~Arakawa & Timasheff, 1991!. Salts that do not have specific binding to proteins increase their thermal stability essentially through their effect on water structure manifested by an increase in its surface tension~Sinanoglu & Abdulnur, 1965;Lin & Timasheff, 1996!. It is suggested that protein stability and solubility are linked to this phenomenon.…”

mentioning

confidence: 99%

A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions

Kaushik

Bhat

1999

Protein Science

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The stability of proteins is known to be affected significantly in the presence of high concentration of salts and is highly pH dependent. Extensive studies have been carried out on the stability of proteins in the presence of simple electrolytes and evaluated in terms of preferential interactions and increase in the surface tension of the medium. We have carried out an in-depth study of the effects of a series of carboxylic acid salts: ethylene diamine tetra acetate, butane tetra carboxylate, propane tricarballylate, citrate, succinate, tartarate, malonate, and gluconate on the thermal stability of five different proteins that vary in their physico-chemical properties: RNase A, cytochrome c, trypsin inhibitor, myoglobin, and lysozyme. Surface tension measurements of aqueous solutions of the salts indicate an increase in the surface tension of the medium that is very strongly correlated with the increase in the thermal stability of proteins. There is also a linear correlation of the increase in thermal stability with the number of carboxylic groups in the salt. Thermal stability has been found to increase by as much as 22 8C at 1 M concentration of salt. Such a high thermal stability at identical concentrations has not been reported before. The differences in the heat capacities of denaturation, DC p for RNase A, deduced from the transition curves obtained in the presence of varying concentrations of GdmCl and that of carboxylic acid salts as a function of pH, indicate that the nature of the solvent medium and its interactions with the two end states of the protein control the thermodynamics of protein denaturation. Among the physico-chemical properties of proteins, there seems to be an interplay of the hydrophobic and electrostatic interactions that lead to an overall stabilizing effect. Increase in surface free energy of the solvent medium upon addition of the carboxylic acid salts appears to be the dominant factor in governing the thermal stability of proteins.

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Stability Studies on Maize Leaf Phosphoenolpyruvate Carboxylase: The Effect of Salts

Cited by 27 publications

References 39 publications

Stabilization effects of kosmotrope systems on ornithine carbamoyltransferase

Stabilization effects of kosmotrope systems on ornithine carbamoyltransferase

Glutamate Counteracts the Denaturing Effect of Urea through Its Effect on the Denatured State

A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions

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