Oxygen binding and subunit equilibria of Busycon hemocyanin

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

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)471-474,IN35,475-479
JournalJournal of Molecular Biology
Volume50
Issue number2
DOIs
StatePublished - Jun 14 1970
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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