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Inversion of the Bohr effect upon oxygen binding to 24-meric tarantula hemocyanin.

Sterner, Reinhard and Decker, H. (1994) Inversion of the Bohr effect upon oxygen binding to 24-meric tarantula hemocyanin. Proceedings of the National Academy of Sciences of the United States of America 91 (11), pp. 4835-9.

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Abstract

The Bohr effect describes the usually negative coupling between the binding of oxygen and the binding of protons to respiratory proteins. It was first described for hemoglobin and provides for an optimal oxygen supply of the organism under changing physiological conditions. Our measurements of both oxygen and proton binding to the 24-meric tarantula hemocyanin establish the unusual case where a ...

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Item type:Article
Date:1994
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
8487305PubMed ID
Classification:
NotationType
AnimalsMESH
BuffersMESH
Hemocyanin/metabolismMESH
Hydrogen-Ion ConcentrationMESH
Oxygen/metabolismMESH
Protein ConformationMESH
ProtonsMESH
SpidersMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:13718
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