Bj. Bequette et al., Vascular sources of phenylalanine, tyrosine, lysine, and methionine for casein synthesis in lactating goats, J DAIRY SCI, 82(2), 1999, pp. 362-377
The contribution to casein biosynthesis of peptides derived from blood was
examined in late lactation goats (254 to 295 d in milk). Ratios of mammary
uptake of free amino acids (AA) in blood to output of AA in milk protein an
d ratios of the enrichments of Phe, Tyr, Met, and Lys at isotopic plateau i
n secreted milk casein to the free AA in arterial and mammary vein blood we
re monitored during the last 5 h of a 30-h continuous i.v. infusion of [1-C
-13]Phe, [H-2(4)]Tyr, [5-(CH3)-C-13]Met, and [2-N-15]Lys on two occasions:
before (control) and on d 6 of an i.v. infusion of Phe (6 g/d). During the
control, uptakes of free Phe and Met were less than their output in milk. T
his result was comparable with the labeling kinetic results, suggesting tha
t vascular peptides contributed 5 to 11% of Phe and 8 to 18% of Met. Free T
yr and Lys uptakes during the control were sufficient for milk output; howe
ver, the labeling kinetics indicated that 13 to 25% of the Tyr and 4 to 13%
of the Lys were derived from peptides. Infusion of Phe increased the uptak
e of free AA but reduced the contribution of peptides toward Phe (0 to 3%)
and Tyr(8 to 14%) supply for casein synthesis. Whole body hydroxylation of
Phe to Tyr increased from 10 to 18% with the infusion of Phe; within the ma
mmary gland, this conversion was lower (3 to 5%). Results suggest that the
mammary utilization of peptides containing Phe and Tyr appears to depend on
the supply of free AA in blood.