Journal of Dairy Research · 1971 · 61 citations · 17 references
Natural SciencesBiochemistryBiophysicsBiophysical ChemistryMilk ChemistryMolecular BiophysicsBiomolecular ElectrostaticsCasein ChemistryElectrostatic Interactions In BiomoleculesElectrostatics In BiomoleculesProtein ElectrophoresisCasein AggregationCasein StabilityElectrophoresisMicellesMilk Casein Micelle Structure
Summary Analytical electrophoresis of native and of rennet-treated casein micelles was carried out at 26 and at 5°C in a sucrose density gradient in a medium of the same ionic composition as milk. Under normal circumstances, the micelles were negatively charged and showed little heterogeneity in the electric field, the fastestmoving ones having at 26°C a mobility not more than 30% greater than that of the slowest. Native micelles were more highly charged at 5 than at 26°C; at each temperature, the mobility was approximately halved by rennet treatment. The results suggest that the effects of rennet treatment and of alterations in temperature on the tendency of the micelles to clot can be entirely explained as being caused by changes in charge.
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Principles of Dairy Chemistry.
William Horwitz · Journal of AOAC INTERNATIONAL · 1960 · 172 citations
Relation Between Micellar and Serum Casein in Bovine Milk
Dyson Rose · Journal of Dairy Science · 1968 · 171 citations · Full text
The ultraviolet absorption spectrum of ribonuclease
David Shugar · Biochemical Journal · 1952 · 161 citations · Full text