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      Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding.

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          Abstract

          Conformational and structural changes of cod myosin at pH 2.5 and 11 and after subsequent pH readjustment to pH 7.5 were studied. Results suggest that on acid unfolding, the myosin rod may fully dissociate due to electrostatic repulsion within the coiled coil, while it does not dissociate at alkaline pH. Both pHs led to significant conformational changes in the globular head fraction of the myosin heavy chains, suggesting that it takes on a molten globular configuration. A large part of the myosin light chains are lost on both pH treatments. On pH readjustment to neutrality, the heavy chains take on a structural form similar to the native state with the coiled-coil rod reassociating from acid pH while leaving the globular head less packed, more hydrophobic and structurally less stable. The irreversible change brought about in the globular head region leads to the failure of light chains to reassemble onto it, a drastic loss in ATPase activity, and more exposure of reactive thiol groups. The acid and alkali processes therefore lead to substantial changes in the globular part of the myosin molecule and perhaps more importantly to different molecular changes in myosin, depending on which pH treatment is employed.

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          Author and article information

          Journal
          J. Agric. Food Chem.
          Journal of agricultural and food chemistry
          American Chemical Society (ACS)
          0021-8561
          0021-8561
          Nov 19 2003
          : 51
          : 24
          Affiliations
          [1 ] Laboratory of Aquatic Food Biomolecular Research, Aquatic Food Products Program, Department of Food Science and Human Nutrition, University of Florida, Gainesville, Florida 32611, USA. hgkristinsson@mail.ifas.ufl.edu
          Article
          10.1021/jf026193m
          14611192
          a8c5aa5f-bac5-4683-9546-9fdaf74d3e6b
          History

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