Chromatograms of buffalo individual milk samples, obtained
using the optimised elution conditions of Bonfatti et al. (2008),
are reported in Fig. 1. All caseins and major whey proteins were
separated simultaneously with high resolution.
j-CN consisted of a number of partially coeluting peaks, which
are to be ascribed to different glycosylated and unglycosylated
forms of this protein fraction. Separation of buffalo caseins by
RP-HPLC has been partially achieved alsobut no j-CN polymorphism was detected. Conversely achieved an improved separation of the casein
fractions relative to that ofand described
the presence of a peak, eluting between those of aS2-CN and aS1-
CN, which was later attributed by mass spectrometry to an alternative
form of j-CN, but without any further characterization. Features
of the peaks of j-CN variants and aS2-CN obtained in our
study were similar to those obtainedbut
resolution was greatly improved. As previously reportedpartial
separation of differently phosphorylated forms of aS2-CN led to
multiple peaks and shoulders. Two alternative forms of aS1-CN
have been detected. Each aS1-CN main form gave rise to a double
peak, which is likely to be ascribed to the different degree of
post-translational phosphorylationb-CN exhibited a unique peak eluting between those of aS1-CN
and a-LA. As for bovine milk (Bonfatti et al., 2008), c-CNs partially
co-eluted with b-CN. a-LA eluted after b-CN and before the peak of
b-Lg.