AJP - Regulatory, Integrative and Comparative Physiology, Vol 267, Issue 1 1-R6, Copyright © 1994 by American Physiological Society

ARTICLES

Utilization of dipeptides by the caprine mammary gland for milk protein synthesis

F. R. Backwell, B. J. Bequette, D. Wilson, A. G. Calder, J. A. Metcalf, D. Wray-Cahen, J. C. MacRae, D. E. Beever and G. E. Lobley
Rowett Research Institute, Bucksburn, Aberdeen, United Kingdom.

Specific use by the mammary gland in vivo of amino acids (AA) of peptide origin has been demonstrated in lactating dairy goats using a dual-labeled tracer technique involving close-arterial (external pudic artery, EPA) infusion of 13C-labeled dipeptides. The extent of utilization does not appear to differ for glycyl-L-[1-13C]phenylalanine and glycyl-L-[1-13C]leucine, perhaps indicative of a common mechanism by which AA are incorporated from peptide into milk protein. [1-13C]phenyl-alanine of peptide origin appears to be concentrated within the red blood cell, suggesting a role for the erythrocyte in peptide metabolism in vivo. In conclusion, it appears that the lactating mammary gland of goats has the ability to utilize AA of peptide origin for milk protein synthesis, and while the mechanism by which [1-13C]AA are incorporated into milk protein is not clear, it may involve peptide hydrolysis by either mammary cell surface or red blood cell hydrolases followed by uptake of liberated AA by the mammary gland.

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