So. Hoskin et al., Does glutamine act as a substrate for transamination reactions in the liver of fed and fasted sheep?, BR J NUTR, 85(5), 2001, pp. 591-597
The present study investigated the relative importance of glutamine as a tr
ansamination source in the ovine liver by examination of the labelling of a
mino acids (AA) in the hepatic free pool, mixed liver and plasma proteins o
f fed and fasted sheep, following infusion of isotopically-labelled glutami
ne. in a cross-over design four sheep were either fasted for 3 d or fed to
1.2 x energy maintenance and finally euthanased. At each intake, the sheep
were infused for 6 h with [2-N-15]glutamine (150 mu mol/h) and samples of t
otal plasma protein isolated. Following the terminal infusion, liver tissue
total proteins were prepared and hydrolysed and N-15-enrichments in sevent
een AA were determined by GC-combustion-isotope-ratio mass spectrometry. Al
l AA were enriched (relative to natural abundance) except lysine and threon
ine, with the lowest enrichments in phenylalanine and histidine. There was
no effect of the fed v. fasted state, except for leucine and isoleucine in
liver protein (P < 0.05). Enrichments in liver protein were greater than in
plasma protein (P < 0.01, except proline) and probably reflect the faster
turnover rate of hepatic constitutive proteins compared with export protein
s. Amination to methionine was greater than that to phenylalanine (P < 0.01
), suggesting a mechanism for preferentially protecting the former. This fa
ctor could be important for ruminant production, as methionine is often con
sidered to be the first limiting AA for animals offered certain silages and
conserved forages. Enrichments in all AA (except for glutamine, alanine an
d aspartate) were less than that for glutamate (P < 0.01), and thus transam
inations may have occurred with glutamine directly or via glutamate, follow
ing the action of hepatic glutaminase.