The cellular uptake of branched-chain amino acids in mammary tissue is impo
rtant for understanding their role in milk synthesis in the sow. This study
characterized the kinetic properties and substrate specificity of the vali
ne uptake system in the porcine mammary gland. Mammary tissue was collected
from lactating sows at slaughter and tissue explants were incubated in med
ia containing isosmotic salt and amino acids of interest, plus [H-3]valine
tracer. Valine uptake was time-dependent and was dependent on the presence
of sodium, as indicated by a reduction in uptake when sodium in the medium
was replaced by choline. The valine transport system in porcine mammary tis
sue had a K-m of 0.64 mM, a V-max of 1.84 mmol.kg cell water(-1).30 min(-1)
, and a K-d (diffusion constant) of 1.16 L.kg cell water(-1).30 min(-1). Va
line uptake was inhibited by leucine and alpha -aminoisobutyric acid and by
high concentrations of L-alanine, L-lysine, cycloleucine, L-glutamine, and
L-methionine, but not by 2-(methyl-amino)-isobutyric acid. This transport
system is the primary system responsible for uptake of valine, and probably
other branched-chain amino acids, in lactating sow mammary tissue. Physiol
ogical concentrations of valine in the blood are below the K-m of the speci
fic valine transport system and well below the diffusion uptake capabilitie
s. The kinetic parameters of this valine transport system should not be lim
iting to valine uptake for milk protein synthesis. However, competition of
valine uptake with branched-chain amino acids, as well as with other amino
acids, may affect valine uptake in lactating tissue.