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Oxygen binding and subunit equilibria of Busycon hemocyanin
Authors:H A DePhillips  K W Nickerson  K F Van Holde
Affiliation:1. Cardiology Division, Department of Medicine, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA;2. Massachusetts General Physicians Organization, Harvard Medical School, Boston, MA, USA;3. Department of Medicine, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA;1. South African National Biodiversity Institute, Kirstenbosch Research Centre, Cape Town, South Africa;2. Centre for Invasion Biology, Department of Botany and Zoology, Stellenbosch University, Stellenbosch, South Africa;3. Royal Botanic Gardens, Kew, Richmond, Surrey TW9 3AE, United Kingdom;1. Institute of Animal Husbandry and Animal Welfare, Department for Farm Animals and Veterinary Public Health, University of Veterinary Medicine, Vienna, Veterinärplatz 1, 1210 Vienna, Austria;2. Division of Livestock Sciences, Department of Sustainable Agricultural Systems, University of Natural Resources and Life Sciences, Vienna, Gregor-Mendel-Straße 33, 1180 Vienna, Austria;3. Department of Applied Statistics, JK University Linz, Altenberger Str. 69, 4040 Linz, Austria;4. Unit of Physiology, Pathophysiology and Experimental Endocrinology, Department for Biomedical Sciences, University of Veterinary Medicine, Vienna, Veterinärplatz 1, 1210 Vienna, Austria;1. Key Laboratory of Animal Protein Deep Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315800, China;2. Food Science & Nutrition Department, Nanjing Normal University, Nanjing 210024, China
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.
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