Human-milk proteins

Analysis of casein and casein subunits by anion-exchange chromatography, gel electrophoresis, and specific staining methods

Bibliographic Data

ID9045780
AuthorsChristine Berg (0000-0003-0392-7840, corresponding author), C Kunz (0000-0002-0511-3915), B Lonnerdal
Year1990
Volume51
Issue1
Pages37-46
Publication date1990-01-01
Peer ReviewedYes
Open AccessYes
TypeARTICLE
VenuePetermanns geographische Mitteilungen (JOURNAL)
Journal identifiersISSN: 0031-6229
PublisherElsevier BV (PUBLISHER)
DOI10.1093/ajcn/51.1.37
OpenAlexW1688683
LanguageEN
References cited44

Casein in human milk is believed to serve several biological functions in newborns. However, the content and subunit composition of human casein has so far received little attention. We recently developed a method to separate human-milk whey and casein by adjustment of whole human milk to pH 4.3 and addition of calcium followed by ultracentrifugation. In this study we analyzed and evaluated human casein prepared by different methods. We used fast protein liquid chromatography (FPLC) with an anion-exchange column (Mono-Q) and polyacrylamide gradient gel electrophoresis techniques to analyze the casein subunit composition. Total casein in human milk, as determined by the Kjeldahl method, varies during lactation; the casein content is approximately 20% of the total protein content in early lactation and 45% in late lactation. We found differences in both glycosylation and phosphorylation patterns of kappa-caseins and beta-caseins from premature and term milk samples.

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