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Protein Purification: Principles and Trends
Title
Protein Purification: Principles and Trends
Editor
iConcept Press
Price
USD$89.00
ISBN
978-1-922227-40-9
Clicks
20060

Chapter 6

Protein Purification: Principles and Trends

Principal Protein Purification and Analysis Led to New Roles of the α1–β1 (and α2–β2) Interface of Human Hemoglobin Molecule

by Yoshiaki Sugawara, Yoko Abe, Ikumi Ikumi Ohgushi, Eriko Ueno, Mai Okazaki, Mai Yamada, Aya Okamoto, Mariko Miyake, Fusako Fukami, Asako Suzuki, Yayoi Yukuta, Etsuko Kadono and Ai Yano

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Abstract

Cellular life is reliant upon rapid and efficient responses to internal and external conditions, whereby basic molecular events associated with these processes are the structural transitions of the proteins (structural protein allostery) involved. The human hemoglobin (Hb) molecule (α2β2) holds a special position in these structural transitions. Hb (α2β2; alternatively, a dimer of αβ protomers) has two types of αβ interface (i.e., α1β1 [and α2β2] and α1β2 [and α2β1]). The latter α1–β2 (and α2–β1) interface is known to be associated with cooperative O2 binding, and exhibits principal roles if the molecule goes from its deoxygenated to oxygenated quaternary structure. However, the role of the former α1–β1 (and α2–β2) interface has been unclear for a long time. In a series of studies, we have examined possible involvement of the α1–β1 (and α2–β2) interface in the oxidative behavior of human Hb (oxidation of ferrous heme iron by bound O2), degradation of the Hb molecule to hemichrome (hemichrome formation), and hemichrome emergence and subsequent formation of Heinz bodies within the erythrocytes. In this chapter, we deliberately aim to deal with necessary basic methods in protein purification and analysis that led us to grasp new roles assigned to the α1–β2 (and α2–β1) interface of the human Hb molecule: one is for stabilizing the HbO2 tetramer against acidic autoxidation; and the other is for controlling the fate (removal) of its own erythrocyte from the blood circulation.

Author Details

Yoshiaki Sugawara
Department of Health Science, Prefectural University of Hiroshima, Japan
Yoko Abe
Department of Health Science, Hiroshima Prefectural Women’s University, Japan
Ikumi Ikumi Ohgushi
Department of Health Science, Hiroshima Prefectural Women’s University, Japan
Eriko Ueno
Department of Health Science, Hiroshima Prefectural Women’s University, Japan
Mai Okazaki
Department of Health Science, Hiroshima Prefectural Women’s University, Japan
Mai Yamada
Department of Health Science, Hiroshima Prefectural Women’s University, Japan
Aya Okamoto
Department of Health Science, Hiroshima Prefectural Women’s University, Japan
Mariko Miyake
Department of Health Science, Hiroshima Prefectural Women’s University, Japan
Fusako Fukami
Department of Health Science, Hiroshima Prefectural Women’s University, Japan
Asako Suzuki
Department of Human Life Science, Hiroshima Women’s University, Japan
Yayoi Yukuta
Department of Human Life Science, Hiroshima Women’s University, Japan
Etsuko Kadono
Department of Human Life Science, Hiroshima Women’s University, Japan
Ai Yano
Department of Human Life Science, Hiroshima Women’s University, Japan

Citation

Yoshiaki Sugawara, Yoko Abe, Ikumi Ikumi Ohgushi, Eriko Ueno, Mai Okazaki, Mai Yamada, Aya Okamoto, Mariko Miyake, Fusako Fukami, Asako Suzuki, Yayoi Yukuta, Etsuko Kadono and Ai Yano. Principal Protein Purification and Analysis Led to New Roles of the α1–β1 (and α2–β2) Interface of Human Hemoglobin Molecule. In Protein Purification: Principles and Trends. ISBN:978-1-922227-40-9. iConcept Press. 2016.

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