pH-Jump of Pepsin Studied by Tyrosine Ionization(Biological Chemistry)

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概要

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• Rapid conformational changes of pepsin occurring within 5s due to pH-jump were studied by the stopped-flow method through the absorption change at 245nm which is caused by the ionization of tyrosine residues. Two distinct phases of conformational change involving the exposure of tyrosine residues, perhaps buried in native pepsin, were observed. The pH profile of absorption change caused by the alkaline denaturation, ΔA, suggests that the unfolding in the slower phase occurs in lower pH than that in faster phase and that tyrosine residues exposed in the faster phase are more perturbed in the folded state than those exposed in the slower phase.

• 社団法人日本農芸化学会の論文
• 1986-05-23

著者

• HIROMI Keitaro

  Department of Food Science and Technology, Faculty of Engineering, Fukuyama University

• Hiromi K

  Department Of Food Science And Technology Faculty Of Agriculture Kyoto University

• Hiromi Keitaro

  Department Of Food Science And Technology Faculty Of Agriculture Kyoto University

• KITAGISHI Keiko

  Department of Food Science and Technology, Faculty of Agriculture, Kyoto University

• Kitagishi K

  Department Of Food Science And Technology Faculty Of Agriculture Kyoto University

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