Essential Binding of LukF of Staphylococcal γ-hemolysin Followed by the Binding of hγII for the Hemolysis of Human Erythrocytes

Toshiko Ozawa; Jun Kaneko; Yoshiyuki Kamio

doi:10.1271/bbb.59.1181

Essential Binding of LukF of Staphylococcal γ-hemolysin Followed by the Binding of hγII for the Hemolysis of Human Erythrocytes

Toshiko Ozawa, Jun Kaneko, Yoshiyuki Kamio

AGR - Agricultural Chemistry

Research output: Contribution to journal › Article › peer-review

31 Citations (Scopus)

Abstract

Staphylococcal γ-hemolysin consists of two protein components, LukF and HγII. This report clarifies the order of binding of the two components to human erythrocytes for the hemolytic activity of the toxin. The initial binding of LukF to the human erythrocytes is essential for the subsequent binding of HγII to the same cells, with the formation of a heat-undissociable protein of about 100 kDa containing LukF and HγII.

Original language	English
Pages (from-to)	1181-1183
Number of pages	3
Journal	Bioscience, Biotechnology, and Biochemistry
Volume	59
Issue number	6
DOIs	https://doi.org/10.1271/bbb.59.1181
Publication status	Published - 1995

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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10.1271/bbb.59.1181

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title = "Essential Binding of LukF of Staphylococcal γ-hemolysin Followed by the Binding of hγII for the Hemolysis of Human Erythrocytes",

abstract = "Staphylococcal γ-hemolysin consists of two protein components, LukF and HγII. This report clarifies the order of binding of the two components to human erythrocytes for the hemolytic activity of the toxin. The initial binding of LukF to the human erythrocytes is essential for the subsequent binding of HγII to the same cells, with the formation of a heat-undissociable protein of about 100 kDa containing LukF and HγII.",

author = "Toshiko Ozawa and Jun Kaneko and Yoshiyuki Kamio",

note = "Funding Information: Acknowledgments. We are grateful to Dr. Y. Sato of Phamaceutical Institute, Tohoku University for his kind advice for preparation of erythrocyte membrane. This work was supported in part by the grants from the Ministry of Education, Science, and Culture of Japan (05304028 and 0667028); The Naito Foundation; and Yamada Science Foundation.",

year = "1995",

doi = "10.1271/bbb.59.1181",

language = "English",

volume = "59",

pages = "1181--1183",

journal = "Bioscience, Biotechnology and Biochemistry",

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publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

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T1 - Essential Binding of LukF of Staphylococcal γ-hemolysin Followed by the Binding of hγII for the Hemolysis of Human Erythrocytes

AU - Ozawa, Toshiko

AU - Kaneko, Jun

AU - Kamio, Yoshiyuki

N1 - Funding Information: Acknowledgments. We are grateful to Dr. Y. Sato of Phamaceutical Institute, Tohoku University for his kind advice for preparation of erythrocyte membrane. This work was supported in part by the grants from the Ministry of Education, Science, and Culture of Japan (05304028 and 0667028); The Naito Foundation; and Yamada Science Foundation.

PY - 1995

Y1 - 1995

N2 - Staphylococcal γ-hemolysin consists of two protein components, LukF and HγII. This report clarifies the order of binding of the two components to human erythrocytes for the hemolytic activity of the toxin. The initial binding of LukF to the human erythrocytes is essential for the subsequent binding of HγII to the same cells, with the formation of a heat-undissociable protein of about 100 kDa containing LukF and HγII.

AB - Staphylococcal γ-hemolysin consists of two protein components, LukF and HγII. This report clarifies the order of binding of the two components to human erythrocytes for the hemolytic activity of the toxin. The initial binding of LukF to the human erythrocytes is essential for the subsequent binding of HγII to the same cells, with the formation of a heat-undissociable protein of about 100 kDa containing LukF and HγII.

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Essential Binding of LukF of Staphylococcal γ-hemolysin Followed by the Binding of hγII for the Hemolysis of Human Erythrocytes

Abstract

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