Abstract
The serum proteins isolated from homogenized milk by centrifugation and exposed to 2152 lx of fluorescent light for 72h were fractionated into the major protein components by gel filtration chromatography. Amino acid composition of the major serum proteins, β-lactoglobulin and α-lactalbumin which accounted for 80% of the total serum protein, did not change substantially following light exposure. Changes in amino acid composition associated with fluorescent light exposure occurred primarily in the high molecular weight fraction of serum proteins. This fraction amounts to at most 10% of the serum proteins.
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