Changes in the Protein Fractions of Human Milk during Lactation

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Abstract
The changes in the absolute and relative contents of α- and ĸ-caseins, lactoferrin, α-lactalbumin, serum albumin and lysozyme in human milk have been studied through the period of lactation. Protein fractions of 209 samples were analyzed by a discontinuous poly-acrylamide gel electrophoresis method, β- and ĸ -caseins decreased from colostrum to mature milk although their relative percentages remained constant. They accounted for 12–15 and 9–13% of the total protein in human milk, respectively. Lactoferrin decreased in absolute and relative amounts with advancing lactation. This protein represented 32–19% of the human milk proteins. α-Lactalbumin slightly decreased from colostrum to transitional milk but there was an increase in mature milk by 16–30 days. The percentages of this protein in colostrum and mature milk were approximately 23 and 30%, respectively. Serum albumin also decreased with advancing lactation, but the differences between transitional and mature milk were not statistically significant. Lysozyme increased from colostrum to mature milk both in relative and absolute amounts. Colostrum contained about 262 µg/ml, and mature milk 1,246 µg/ml, representing 1.5 and 12.1% of total milk proteins.

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