Proteins of human milk. I. Identification of major components.

Abstract

Abstract Traditionally, human milk proteins are identified largely by reference to bovine milk. Hence, to identify the major proteins in human milk, we subjected human and bovine milk, in parallel, to high-resolution two-dimensional electrophoresis. Isoelectric precipitation at pH 4.6 was our criterion for distinguishing whey proteins from those of the casein complex. The alpha- and beta-caseins were identified on the basis of relative abundance, relative molecular mass, and relative isoelectric points. Kappa casein was identified as a series of four spots, which disappear from bovine skim milk treated with rennin (chymosin; EC 3.4.23.4) during the clotting process. Para kappa-casein does not appear on the standard ISO-DALT pattern after treatment of bovine milk with rennin, but does appear in BASO-DALT pattern, indicating its high isoelectric point. No protein disappeared from ISO-DALT patterns of human milk after rennin treatment, and no new protein comparable to bovine para kappa-casein appeared in the BASO-DALT patterns; this suggests that kappa-casein is absent from human milk. The proteins identified in human milk patterns include the alpha and beta casein families, lactalbumin, albumin, transferrin, IgA, and lactoferrin. Numerous additional proteins seen in patterns for human milk remain to be identified.