Equilibrium and kinetic study of sodium‐and potassium‐induced conformational changes of apo‐α‐lactalbumin

Y. HIRAOKA, S. SUGAI

研究成果: Article査読

60 被引用数 (Scopus)

抄録

Equilibrium and kinetics of Na+‐and K+‐induced conformational changes of apo‐α‐lactalbumin were studied by means of circular dichroism. While apo‐α‐lactalbumin was considerably unfolded in the absence of Na+ or K+ in 20 mM Tris at pH 8.0 and 25°, both the monovalent cations restored the tertiary structure of the protein. Apparent binding constants of Na+ and K+ to the apoprotein were estimated from the equilibria of the Na+‐ and K+‐induced conformational changes. Based on kinetic data of the conformational changes induced by the monovalent cations, binding mechanism of the ions to the apo‐protein was examined. Bound alkali‐metal ions stabilize the native‐like state and an activated state in the unfolding‐refolding reaction of the apoprotein.

本文言語English
ページ(範囲)252-261
ページ数10
ジャーナルInternational Journal of Peptide and Protein Research
26
3
DOI
出版ステータスPublished - 1985 9
外部発表はい

ASJC Scopus subject areas

  • 生化学

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