Kappa-casein as purified from bovine milk exhibits a rather unique disulfid
e bonding pattern as revealed by SDS-PAGE. The disulfide bonded caseins pre
sent, range from dimer to octamer and above and preparations contain about
10% monomer. All of these heterogeneous polymers, however, self-associate i
nto 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 t
hese spherical particles. Treatment with EDTA causes disruption of the kapp
a-casein particles and leads to a broader size distribution as judged by el
ectron microscopy, dynamic light scattering and analytical ultracentrifugat
ion. The size and shape of the particles are in accord with earlier propose
d 3D models for kappa-casein, that actually predicted participation of diva
lent cations in the structure. Published by Elsevier Science Ltd.