The occurrence and subcellular distribution of ornithine-delta-aminotr
ansferase have been studied in lactating bovine mammary glands. The en
zyme is localized in the mitochondria and has a unique thermal reactio
n profile that distinguishes it from putative liver and kidney isozyme
s. The enzyme concentration in the gland correlates well with a role i
n the conversion of ornithine into the proline precursor, L-Delta(1)-p
yrroline-5-carboxylate. However, an unusually high Michaelis constant
for the mitochondrial enzyme (8.4 mM) raises the question of enzyme ef
ficiency in vivo such that this pathway needs to be considered in esti
mating barriers to protein secretion into milk.