Title : [Changes in the immunochemical properties of beta-lactoglobulin during proteolysis and exposure to various physico-chemical factors].

Pub. Date : 1990 Sep-Oct

PMID : 2251783






1 Functional Relationships(s)
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1 Heating of cow milk beta-lactoglobulin at 96 degrees, pH 8.0 led to the protein aggregation because of intermolecular disulfide exchange as shown by agarose gel immunoelectrophoresis, where additional precipitation strips were detected. Disulfides beta-lactoglobulin Bos taurus