The interaction of inorganic mercury with human and bovine milk protei
ns was studied, Gel filtration chromatography of skimmed milk and whey
incubated with mercury showed that, in human milk, mercury was mainly
bound to caseins, while a low proportion was bound to albumin, In bov
ine milk, mercury was associated with two protein fractions, caseins a
nd beta-lactoglobulin. Furthermore, it was shown by electrophoresis th
at mercury induced the formation of dimers of beta-lactoglobulin, Thus
, in both human and bovine milk, mercury prossessed greater ability to
interact with milk proteins than to the low-molecular-weight substanc
es, However, the pattern of mercury distribution was different between
the milk of these two species.