I. The fractional synthetic rates of tissue proteins were studied in growing pigs using the constant-infusion technique of tracer-labelled amino acids ( [l4C]1eucine and [14C]lysine) and the mathetmatical model for calculation, employed in rats by Garlick, Millward &James (1973).2 . During a 6 h infusion, samples were taken from blood and muscle and at the end of the infusion from liver, muscle, pancreas, heart, duodenum, jejunum, ileum, colon, and skin. The specific radioactivity of free and protein-bound leucine and lysine was estimated. 3. A quasi-steady-state in the specific radioactivity of free plasma leucine and lysine was reached within approximately z h, the rate-constants being 35 and 48/d respectively.4. The specific radioactivity of free leucine and lysine in plasma was used to calculate the flux of these amino acids. It was found to be higher than the daily intake.5. The average fractional rate of protein synthesis in muscle and heart was 8.1 %/d, in small and large intestine the values were 50 and 33 %/d respectively and in liver and pancreas more than Ioo%/d.6. The calculation of protein synthetic rate in pig tissue using the constant-infusion method of labelled amino acids seems to be a suitable tool for study of this species.

1. The effects of thyroid hormones on the range of tissue protein synthesis in growing pigs using the constant infusion technique with [14C]leucine and [I4C]lysine were studied.2. During a 6 h infusion, samples were taken from blood and, at the end of the infusion, from liver, pancreas, stomach, small and large intestines, kidney cortex, kidney medulla, muscle and skin.3. Lower relative specific radioactivities of free leucine and lysine in several tissues were observed in the hormone-treated group than in the untreated one.4. The range of protein synthesis rate and the daily amount of protein synthesized in tissues was higher in all tissues after application of thyroid hormones.5. Assuming that the organs analysed represented 70 % of the total trichloroacetic acid-precipitable protein of the pig, the estimated range of daily protein synthesis was 251490 and 312-88Og in untreated and hormone-treated pigs respectively.

No abstract

A trial was performed with 2 fistula pigs (each with 2 fistulas, one located about 30 cm below the pyloric orifice and the other at the end of the small intestine). Animal A received a casein diet containing 14% crude protein for a period of 2 weeks before the tracer amino acid was administered. Animal B received the same diet for a period of 10 days and was then fed a diet (at the same protein level) containing gluten as sole protein source. The two tracer amino acids, 14C-U-L-leucine and 3H-4,5-(N)-L-lysine, were injected intravenously. The passage rates for dry matter, organic matter and N measured at the beginning of the small intestine were higher than the rate of intake. The rate of passage of amino acids was also found to be increased relative to the rate of intake. In general, this increase involved the non-essential amino acids to a much larger extent. A considerable proportion of the amino acids passing into the large intestine is not excreted with the faeces but is probably converted in catabolic processes. It is for this reason that any values for the efficiency of amino acid absorption calculated on the basis of data on the faecal excretion of amino acids will not provide conclusive evidence for the availability of dietary amino acids in processes of the intermediate metabolism. The rate of secretion of 3H and 14C radioactivity into the digesta of the small intestine was found to increase rapidly within 1-2 hrs after administration of the tracer amino acids. The 14C radioactivity detected was found to be almost exclusively derived from 14C leucine while only about 60% of the 3H activity found in the digesta of fistula I were shown to be bound to lysine. Labelled lysine and leucine (of endogenic origin) are absorbed into the small intestine at a slower rate (i.e. endogenic proteins are less efficiently digested) than the non-radioactive amino acids (of exogenic origin) so that a process of concentration of endogenic amino acids is observed towards the end of the small intestine.