Isolation and characterization of a 21 kDa whey protein in rhesus monkey (Macaca mulatta) milk.
A soluble protein in Rhesus monkey milk was isolated to apparent homogeneity by FPLC gel filtration, anion-exchange and reverse-phase chromatography. It is a major milk protein and is present at 2.5-3.0 mg/ml milk throughout lactation. It is only found in the whey fraction of milk; acid precipitation of casein does not result in any significant change in its concentration. A molecular weight (MW) of about 21.6 kDa was estimated from gel filtration and SDS gel electrophoresis and also calculated from its amino acid composition. The amino acid composition of this protein is similar to that of bovine beta-lactoglobulin (beta-Lg), but it is larger in size, possibly representing a family of primate beta-Lgs.
Department of Nutrition, University of California, Davis.
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Kunz
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Lönnerdal
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D008253:Macaca mulatta; D008894:Milk Proteins / Q000737:chemistry / Q000302:isolation & purification*; D008970:Molecular Weight; D000067816:Whey Proteins
D000596:Amino Acids; D008894:Milk Proteins; D000067816:Whey Proteins