Oxygen binding and subunit equilibria of Busycon hemocyanin

H. A. dePhillips; K. W. Nickerson; K. E. Van Holde

doi:10.1016/0022-2836(70)90205-6

Oxygen binding and subunit equilibria of Busycon hemocyanin

H. A. dePhillips, K. W. Nickerson, K. E. Van Holde

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49 Scopus citations

Abstract

The subunit size of Busycon hemocyanin has been, examined as a function of pH and percentage oxygenation. It was found that at pH 8.2 the 60 s subunit and its 100 s dimer are in equilibrium and that the position of this equilibrium is determined by the number of oxygen molecules bound. Also the oxygenated and deoxygenated 100 s forms were shown by circular dichroic and sedimentation studies to be conformationally distinct. These results are discussed in terms of recent theories of ligand-mediated changes in subunit aggregation in extended protein systems.

Original language	English (US)
Pages (from-to)	471-474,IN35,475-479
Journal	Journal of Molecular Biology
Volume	50
Issue number	2
DOIs	https://doi.org/10.1016/0022-2836(70)90205-6
State	Published - Jun 14 1970
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/0022-2836(70)90205-6

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title = "Oxygen binding and subunit equilibria of Busycon hemocyanin",

abstract = "The subunit size of Busycon hemocyanin has been, examined as a function of pH and percentage oxygenation. It was found that at pH 8.2 the 60 s subunit and its 100 s dimer are in equilibrium and that the position of this equilibrium is determined by the number of oxygen molecules bound. Also the oxygenated and deoxygenated 100 s forms were shown by circular dichroic and sedimentation studies to be conformationally distinct. These results are discussed in terms of recent theories of ligand-mediated changes in subunit aggregation in extended protein systems.",

author = "dePhillips, {H. A.} and Nickerson, {K. W.} and {Van Holde}, {K. E.}",

note = "Funding Information: This work was supported in part by U.S. Public Health Service Research Grants HE-11671 and HE-12326. One of us (K.W.N.) wishes to acknowledge a U.S. Public Health Service Postdoctoral Fellowship 5-FOl-GM-29,756. The assistance of Mr J. Zavitkovski in some of the experiments, and the co-operation of the staff of the Marine Biological Laboratory is appreciated.",

year = "1970",

month = jun,

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doi = "10.1016/0022-2836(70)90205-6",

language = "English (US)",

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pages = "471--474,IN35,475--479",

journal = "Journal of Molecular Biology",

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T1 - Oxygen binding and subunit equilibria of Busycon hemocyanin

AU - dePhillips, H. A.

AU - Nickerson, K. W.

AU - Van Holde, K. E.

N1 - Funding Information: This work was supported in part by U.S. Public Health Service Research Grants HE-11671 and HE-12326. One of us (K.W.N.) wishes to acknowledge a U.S. Public Health Service Postdoctoral Fellowship 5-FOl-GM-29,756. The assistance of Mr J. Zavitkovski in some of the experiments, and the co-operation of the staff of the Marine Biological Laboratory is appreciated.

PY - 1970/6/14

Y1 - 1970/6/14

N2 - The subunit size of Busycon hemocyanin has been, examined as a function of pH and percentage oxygenation. It was found that at pH 8.2 the 60 s subunit and its 100 s dimer are in equilibrium and that the position of this equilibrium is determined by the number of oxygen molecules bound. Also the oxygenated and deoxygenated 100 s forms were shown by circular dichroic and sedimentation studies to be conformationally distinct. These results are discussed in terms of recent theories of ligand-mediated changes in subunit aggregation in extended protein systems.

AB - The subunit size of Busycon hemocyanin has been, examined as a function of pH and percentage oxygenation. It was found that at pH 8.2 the 60 s subunit and its 100 s dimer are in equilibrium and that the position of this equilibrium is determined by the number of oxygen molecules bound. Also the oxygenated and deoxygenated 100 s forms were shown by circular dichroic and sedimentation studies to be conformationally distinct. These results are discussed in terms of recent theories of ligand-mediated changes in subunit aggregation in extended protein systems.

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Oxygen binding and subunit equilibria of Busycon hemocyanin

Abstract

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