Journal of Dairy Science · 1968 · 155 citations · 10 references
AgricultureBiochemistryFood ScienceMilk ChemistryProtein BiochemistryProtein FoldingCasein ChemistryDisulfide Bond FormationMilk Heat StabilityMilk ProteinsPhysicochemical Properties Of MilkCasein Heat StabilityDenaturationDisulfide ContributionsDisulfide LinkersHeat-induced DenaturationHeat-induced Protein AggregationHeat-induced Protein Denaturation
The primary and secondary stages of the heat denaturation of bovine fl-laetoglobulin A have been examined using starch gel electrophoresis and sedimentation velocity techniques. The primary reaction results in the formation of a series of molecular aggregates through the establishment of intermoleeular disulfide bonds. A much heavier component is formed during the secondary reaction, but disulfide bonds are not involved in its formation. The results of turbidity experiments indicated that the susceptibility of the genetic variants of fl-lactogIobulin to heat denaturation is in the order fi--C > fi--B > B--A. Tbe relative importance of the fornmtion of disulfide bonds during the aggregation of each variant is discussed. A mechanism describing the behavior during heat treatment is presented.
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The Sulfur Chemistry of Proteins
R. Cecil, J.R. McPhee · Advances in protein chemistry · 1959 · 317 citations
GENETIC CONTROL OF TWO PRE-ALBUMINS IN PIGS
F. K. Kristjansson · Genetics · 1963 · 207 citations · Full text
Effect of pH on β-Lactoglobulins
H.A. McKenzie, William H. Sawyer · Nature · 1967 · 188 citations
Heat Denaturation of β-Lactoglobulins A and B
Patricia Gough, Robert Jenness · Journal of Dairy Science · 1962 · 102 citations · Full text