Quantitation of the major human whey proteins and isolation of the remaining whey protein fraction by immunoaffinity chromatography

L. R. Woodhouse, B. Lonnerdal

Research output: Contribution to journalArticle

Abstract

The whey proteins of human milk have important nutritional and physiological roles for the breast-fed infants. Approximately 75% of the whey proteins have been identified. The remaining 25% consists of proteins of physiological significance, necessitating further characterization. In this study, mature milk (M) and colostrum (C) samples were quantified for total N, total protein, whey protein, and non-protein N (NPN) using Kjeldahl analysis and Bio-Rad protein determination. Contents of the major whey proteins, lactoferrin (Lf), secretory IgA (sIgA), α-lactalbumin (LA), lysozyme (Lys), and serum albumin (SA) were determined by immunoelectrophoresis and immunodiffusion. Total N for M and C was 1.6 and 3.2 mg/ml, with NPN values of 0.34 and 0.64 mg/ml. Whey protein in M was 6.7 and in C 18.1 mg/ml. Values for M whey proteins were 1.60, 0.81, 1.97, 0.18 ad 0.52 mg/ml for Lf, sIgA, LA, Lys, and SA, respectively, with C whey values of 7.75, 4,89, 2,54 , 0.10, and 0.37. Thus the mature whey consists of 75.7% major proteins, leaving 24.3% minor proteins, and 86.5% major and 13.5% minor proteins in C. For further characterization of the minor protein fraction, immunoaffinity chromotography was applied to obtain a whey sample devoid of the major whey proteins. This whey compartment ws further characterized by gel electrophoresis, crossed immunoelectrophoresis, ion exchange chromatography and gel filtration chromatography.

Original languageEnglish (US)
JournalFederation Proceedings
Volume44
Issue number5
StatePublished - 1985

ASJC Scopus subject areas

  • Medicine(all)

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