Abstract
A zonal ultracentrifuge was used to isolate the heat-induced complexes of β-lactoglobulin and κ-casein. The complexes formed at 80C in sodium cacodylate buffer, pH 6.65, ionic strength 0.08, varied in size and composition, but moved as a single band in starch-gel electrophoresis. The maximum ratio in the complex was estimated to be 3 β-lactoglobulin:1 κ-casein. When a 1:1 mixture was heated at 110C the major component banded in 6.9% sucrose, had a sedimentation coefficient of 2.35, and moved as a single band in starch gel. At 140C, κ-casein was degraded extensively, and no complex could be detected. The complex formed at 90C from a 1:1 mixture in a synthetic serum containing calcium had a sedimentation coefficient of 39. For other mixtures in the presence of calcium the unreacted proteins could not be quantitatively separated from the complex. Zonal ultracentrifugation of heated skimmilk and colloidal calcium phosphate free milk failed to show a discrete complex peak.
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