Hm. Farrell et al., PARTICLE SIZES OF PURIFIED KAPPA-CASEIN - METAL EFFECT AND CORRESPONDENCE WITH PREDICTED 3-DIMENSIONAL MOLECULAR-MODELS, Journal of protein chemistry, 15(5), 1996, pp. 435-445
kappa-Casein as purified from bovine milk exhibits a rather unique dis
ulfide bonding pattern as revealed by SDS-PAGE. The disulfide-bonded c
aseins 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 aver
age radius of 8.9 nm as revealed by negatively stained transmission el
ectron micrographs. Evidence is presented that multivalent cations pla
y a role in the stabilization of these spherical particles. Treatment
with EDTA causes disruption of the kappa-casein particles and leads to
a broader size distribution as judged by electron microscopy and dyna
mic light scattering. The size and shape of the particles are in accor
d with earlier proposed 3D models for kappa-casein that actually predi
cted participation of divalent cations in the structure.