Abstract
κ-Casein as purified from bovine milk exhibits a rather unique disulfide bonding pattern as revealed by SDS-PAGE. The disulfide-bonded caseins present range from dimer to octamer and above and preparations contain about 10% monomer. All of these heterogenous polymers, however, self-associated into nearly spherical uniform particles with an average radius of 8.9 nm as revealed by negatively stained transmission electron micrographs. Evidence is presented that multivalent cations play a role in the stabilization of these spherical particles. Treatment with EDTA causes disruption of theκ-casein particles and leads to a broader size distribution as judged by electron microscopy and dynamic light scattering. The size and shape of the particles are in accord with earlier proposed 3D models forκ-casein that actually predicted participation of divalent cations in the structure.
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Farrell, H.M., Kumosinski, T.F., Cooke, P.H. et al. Particle sizes of purified κ-casein: Metal effect and correspondence with predicted three-dimensional molecular models. J Protein Chem 15, 435–445 (1996). https://doi.org/10.1007/BF01886850
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DOI: https://doi.org/10.1007/BF01886850