Abstract
In order to evaluate some chemical and antigenic properties of α-lactalbumin (α-La) by the treatment with various proteases, the present study was carried out.
After the treatment of α-La with pepsin for 2 hr, α-La was fractionated by Sephadex G-50 column chromatography and the fractions A-D were obtained. Polyacrylamide gel electrophoregrams were extremely resemble between native α-La and B-fraction, but they were remarkably different from the electrophoregram of A-fraction. The molecular weight of A-fraction was greater than that of native α-La, whereas the antigenic activity of A-fraction was 10-25% of the antigenic activity of native α-La. By the treatment with trypsin and chymotrypsin for 2 hr, a-e and a-e fractions were obtained, respectively. Antigenic activity of a-fraction was equal to that of native α-La, but a-fraction was 50% of the native α-La in its antigenic activity.
