A study of polymorphism in milk proteins from local and imported dairy sheep in Australia by capillary electrophoresis

Casein and whey protein fractions of milk obtained from 47 ewes of five breeds or crossbreeds (Awassi, Merino, East Friesian×Merino, Awassi×Merino and Awassi×East Friesian) were analysed by capillary electrophoresis (CE). The experiments were performed on a Beckman P/ACE™ system 5510 with an uncoated fused-silica capillary and a low pH buffer containing urea and a polymeric additive. The four major caseins (αs1-, αs2-, β- and κ  -casein) in an acid precipitate were well separated, as were the two whey proteins, αα-lactalbumin (α-La) and β-lactoglobulin (β-Lg). The electromigration of the proteins was in the order of α-La, β-Lg, αs2-CN, αs1-CN, κ-CN and β  -CN. The milk samples were composed of the same variant of αα-La and two different genotypes (A and B) of β-Lg while the β-Lg AB genotype was evident in the milk of some animals. The αs1-CN fractions displayed considerable heterogeneity with at least 4 different peaks, representing 4 different variants. A fifth peak, corresponding to the Welsh variant (or αs1-CN D), was present in 90% of the ewes’ milk samples. The κ-CN fraction was resolved as a single peak, while the β-CN revealed significant heterogeneity with 3 variants. It appears that the presence of the αs1-CN Welsh variant in Merino ewe and its crosses with Awassi and East Friesian ewes adversely affected milk composition and yield.