ORIGINAL PAPER
Incorporation of endogenous urea nitrogen into amino acids of milk in goats fed diets with various protein levels
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1
The Kielanowski Institute of Animal Physiology and Nutrition, Polish Academy of Sciences, 05-110 Jabłonna, Poland
2
University of Warmia and Mazury, Department of Animal Nutrition and Feed Management, Oczapowskiego 5,10-718 Olsztyn, Poland
Publication date: 2014-08-20
Corresponding author
J. P. Michalski
The Kielanowski Institute of Animal Physiology and Nutrition, Polish Academy of Sciences, 05-110 Jabłonna, Poland
J. Anim. Feed Sci. 2014;23(3):212-216
KEYWORDS
ABSTRACT
The aim of the study was to estimate how much endogenous
urea nitrogen (EUN) was incorporated into various amino acids of milk protein
when goats were fed low (LP), medium (MP), or high protein (HP) diets in
a 3 × 3 Latin-square design. Three Alpine goats of about 35 kg body weight
fitted with a catheter into the jugular vein were fed isoenergetic diets containing
11% (LP), 13% (MP), or 16% (HP) crude protein in dry matter. They were
continuously infused with 15N urea into the jugular vein for 6 days. Daily milk
yield was 1.58, 1.49 and 1.77 g. Milk urea concentrations were 139, 342 and
451 mg · l–1, whereas plasma urea was 178, 356 and 667 mg · l–1 in groups
LP, MP and HP, respectively. Samples of milk protein were hydrolysed with
6 M HCl, and then free amino acids were converted into butyl derivatives using
HCl in butanol, followed by N-acylation using trifluoroacetic acid anhydride. The
amino acid derivatives were analysed using a gas chromatograph equipped
with a mass detector. 15N-excess after a six-day infusion of labelled urea was
significantly higher (P < 0.05) in the vast majority of amino acids of milk protein
from goats fed the LP diet in comparison with goats fed the HP diet. Therefore,
the protein level of diets affects the incorporation of EUN into amino acids of
milk protein. EUN was incorporated primarily into glutamic acid, methionine
and arginine. At all levels of nitrogen in the diets, the incorporation of 15N into
phenylalanine was very low.
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