Lead ion effect on creatine kinase: equilibrium and kinetic studies of inactivation and conformational changes

Zhou, Hongwei; Park, Yong‐Doo; Zhou, Hai‐Meng

doi:10.1016/s1357-2725(01)00145-5

Cited by 5 publications

(2 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For benzyl alcohol, 0.9% (w/v) represents the antimicrobial concentration generally used in protein formulations (). In fluorescence measurements, to detect partially unfolded states of proteins, ANS is generally used at ANS:protein molar ratios of 10−70 ( − ), but at concentrations sufficiently low that the “inner filter” effect in fluorescence is not introduced. Thus, when ANS is used as a probe for partially unfolded protein molecules, typically micromolar concentrations are used.…”

Section: Methodsmentioning

confidence: 99%

Temperature Dependence of Benzyl Alcohol- and 8-Anilinonaphthalene-1-sulfonate-Induced Aggregation of Recombinant Human Interleukin-1 Receptor Antagonist

et al. 2006

View full text Add to dashboard Cite

The critical role played by temperature in ligand-induced protein aggregation was investigated. Recombinant human interleukin-1 receptor antagonist (rhIL-1ra) and the ligands benzyl alcohol and 8-anilinonaphthalene-1-sulfonate (ANS) were used. We investigated aggregation kinetics and the conformation and cysteine reactivity of rhIL-1ra in buffer alone or in the presence of 0.9% (w/v) benzyl alcohol or 4.2 or 21 mM ANS at 25 and 37 degrees C. In buffer, protein aggregation was not detected at 25 degrees C but occurred at 37 degrees C. At 25 degrees C, neither benzyl alcohol nor 4.2 mM ANS enhanced aggregation. However, at 37 degrees C, both compounds greatly accelerated protein aggregation. With 21 mM ANS, rhIL-1ra aggregation was accelerated at both temperatures, but the effect was more pronounced at 37 degrees C than at 25 degrees C. Increasing the temperature from 25 to 37 degrees C caused a minor perturbation in the tertiary structure of rhIL-1ra in buffer but no detectable alteration in secondary structure. Benzyl alcohol enhanced the tertiary structural perturbation at 37 degrees C, but the secondary structure was not affected by the ligand. The reactivity of buried free cysteines of rhIL-1ra was enhanced by benzyl alcohol at 37 degrees C but not at 25 degrees C, consistent with the structural results. Isothermal titration calorimetry documented that the interaction of benzyl alcohol with rhIL-1ra was hydrophobic and that the degree of hydrophobic interactions increased with temperature. At 25 degrees C, the interaction of ANS with rhIL-1ra was electrostatic, but at 37 degrees C, both electrostatic and hydrophobic interactions were important. Taken together, our results support the conclusion that benzyl alcohol and ANS interact hydrophobically with partially unfolded aggregation-prone protein molecules, resulting in temperature-dependent increases in their levels and acceleration of protein aggregation.

show abstract

Section: Methodsmentioning

confidence: 99%

Temperature Dependence of Benzyl Alcohol- and 8-Anilinonaphthalene-1-sulfonate-Induced Aggregation of Recombinant Human Interleukin-1 Receptor Antagonist

et al. 2006

View full text Add to dashboard Cite

show abstract

“…For this reason, it is interesting to study the roles of Pb 2+ on enzymes in aquatic organisms in accordance with ocean pollution [23]. In the case of creatine kinase (ATP: creatine kinase N-phosphotransferase, EC 2.7.3.2), which catalyzes the analogous reaction, Pb 2+ directly induces the loss of creatine kinase activity accompanied by structural unfolding and hydrophobic exposure [24]. Pb 2+ -mediated enzyme folding, including hydrophobic exposure and the aggregation of ocean invertebrate enzymes, may represent an important area of research interest.…”

Section: Introductionmentioning

confidence: 99%

Molecular dynamics simulations integrating kinetics for Pb2+-induced arginine kinase inactivation and aggregation

Lee

Cai

et al. 2015

Process Biochemistry

View full text Add to dashboard Cite

In vitro effects of lead ions on peripheral benzodiazepine receptors and adenylyl cyclase activity in the mantle of Mytilus galloprovincialis

Giannaccini

Betti

Palego

et al. 2004

Comparative Biochemistry and Physiology Part C: Toxicology &

View full text Add to dashboard Cite

Lead ion effect on creatine kinase: equilibrium and kinetic studies of inactivation and conformational changes

Cited by 5 publications

References 25 publications

Temperature Dependence of Benzyl Alcohol- and 8-Anilinonaphthalene-1-sulfonate-Induced Aggregation of Recombinant Human Interleukin-1 Receptor Antagonist

Temperature Dependence of Benzyl Alcohol- and 8-Anilinonaphthalene-1-sulfonate-Induced Aggregation of Recombinant Human Interleukin-1 Receptor Antagonist

Molecular dynamics simulations integrating kinetics for Pb2+-induced arginine kinase inactivation and aggregation

In vitro effects of lead ions on peripheral benzodiazepine receptors and adenylyl cyclase activity in the mantle of Mytilus galloprovincialis

Contact Info

Product

Resources

About