Binding of carbon-monoxide to Alpha-Hemocyanin and Beta-Hemocyanin from Helix-pomatia

Harry A. Kuiper; Ruurd Torensma; Ernst J. Van Bruggen

doi:10.1111/j.1432-1033.1976.tb10829.x

Binding of carbon-monoxide to Alpha-Hemocyanin and Beta-Hemocyanin from Helix-pomatia

Harry A. Kuiper, Ruurd Torensma, Ernst J. Van Bruggen

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Abstract

The binding of carbon monoxide to α and β-hemocyanin from the snail Helix pomatia was studied under equilibrium conditions. Homotropic interactions upon carbon monoxide binding were much weaker than upon the binding of oxygen. Heterotropic interactions (Bohr effect and calcium-ion effect), however, were just as strong as in the case of the binding of oxygen. For α-hemocyanin a linkage has been observed between the binding of carbon monoxide and a change in quaternary structure of the protein

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Original language	English
Pages (from-to)	425-430
Number of pages	6
Journal	European Journal of Biochemistry
Volume	68
Issue number	2
DOIs	https://doi.org/10.1111/j.1432-1033.1976.tb10829.x
Publication status	Published - 1976

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10.1111/j.1432-1033.1976.tb10829.x

Binding of Carbon Monoxide to α-Hemocyanin and β-Hemocyanin from Helix pomatiaFinal publisher's version, 431 KBLicence: Taverne

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title = "Binding of carbon-monoxide to Alpha-Hemocyanin and Beta-Hemocyanin from Helix-pomatia",

abstract = "The binding of carbon monoxide to α and β-hemocyanin from the snail Helix pomatia was studied under equilibrium conditions. Homotropic interactions upon carbon monoxide binding were much weaker than upon the binding of oxygen. Heterotropic interactions (Bohr effect and calcium-ion effect), however, were just as strong as in the case of the binding of oxygen. For α-hemocyanin a linkage has been observed between the binding of carbon monoxide and a change in quaternary structure of the proteinREFERENCES",

author = "Kuiper, {Harry A.} and Ruurd Torensma and {Van Bruggen}, {Ernst J.}",

year = "1976",

doi = "10.1111/j.1432-1033.1976.tb10829.x",

language = "English",

volume = "68",

pages = "425--430",

journal = "European Journal of Biochemistry",

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TY - JOUR

T1 - Binding of carbon-monoxide to Alpha-Hemocyanin and Beta-Hemocyanin from Helix-pomatia

AU - Kuiper, Harry A.

AU - Torensma, Ruurd

AU - Van Bruggen, Ernst J.

PY - 1976

Y1 - 1976

N2 - The binding of carbon monoxide to α and β-hemocyanin from the snail Helix pomatia was studied under equilibrium conditions. Homotropic interactions upon carbon monoxide binding were much weaker than upon the binding of oxygen. Heterotropic interactions (Bohr effect and calcium-ion effect), however, were just as strong as in the case of the binding of oxygen. For α-hemocyanin a linkage has been observed between the binding of carbon monoxide and a change in quaternary structure of the proteinREFERENCES

AB - The binding of carbon monoxide to α and β-hemocyanin from the snail Helix pomatia was studied under equilibrium conditions. Homotropic interactions upon carbon monoxide binding were much weaker than upon the binding of oxygen. Heterotropic interactions (Bohr effect and calcium-ion effect), however, were just as strong as in the case of the binding of oxygen. For α-hemocyanin a linkage has been observed between the binding of carbon monoxide and a change in quaternary structure of the proteinREFERENCES

U2 - 10.1111/j.1432-1033.1976.tb10829.x

DO - 10.1111/j.1432-1033.1976.tb10829.x

M3 - Article

SN - 0014-2956

VL - 68

SP - 425

EP - 430

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

IS - 2

ER -

Binding of carbon-monoxide to Alpha-Hemocyanin and Beta-Hemocyanin from Helix-pomatia

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