Unfolding rates of globular proteins determined by kinetics of proteolysis

Taiji Imoto, Hidenori Yamada, Tadashi Ueda

研究成果: Contribution to journalArticle査読

81 被引用数 (Scopus)

抄録

A convenient method for the determination of unfolding rates of small globular proteins under physiological conditions was developed using digestion with proteases. The apparent first-order rate constants for digestion of lysozyme with thermolysin and with Pronase at pH 8 and 50 °C were shown to be saturated with increases of concentrations of these proteases. The maximum rate constants extrapolated were identical in digestions with two different proteases, and were found to be equal to the unfolding rate constant of lysozyme. Similarly, the unfolding rate constant of RNase A at pH 8 and 50 °C, and those of lysozyme, RNase A and β-lactoglobulin at pH 8 and 40 °C, were determined by the digestion method. Thus, it was shown that digestion by proteases proceeds mainly via the unfolded state of proteins.

本文言語英語
ページ(範囲)647-649
ページ数3
ジャーナルJournal of Molecular Biology
190
4
DOI
出版ステータス出版済み - 8 20 1986

All Science Journal Classification (ASJC) codes

  • 構造生物学
  • 分子生物学

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