Absorption Of Lysine Research Articles

Protein recycling in growing rabbits: contribution of microbial lysine to amino acid metabolism

To study the absorption of microbial lysine in growing rabbits, a labelled diet (supplemented with (15)NH4Cl) was administered to six animals (group ISOT); a control group (CTRL, four rabbits) received a similar, but unlabelled, diet. Diets were administered for 30 d. An additional group of six animals were fed the unlabelled diet for 20 d and then the labelled diet for 10 d while wearing a neck collar to avoid caecotrophy (group COLL), in order to discriminate it from direct intestinal absorption. At day 30 animals were slaughtered and caecal bacteria and liver samples taken. The (15)N enrichment in amino acids of caecal bacteria and liver were determined by GC-combustion/isotope ratio MS. Lysine showed a higher enrichment in caecal microflora (0.925 atom% excess, APE) than liver (0.215 APE) in group ISOT animals, confirming the double origin of body lysine: microbial and dietary. The COLL group showed a much lower enrichment in tissue lysine (0.007 (se 0.0029) APE for liver). Any enrichment in the latter animals was due to direct absorption of microbial lysine along the digestive tract, since recycling of microbial protein (caecotrophy) was avoided. In such conditions liver enrichment was low, indicating a small direct intestinal absorption. From the ratio of [(15)N]lysine enrichment between liver and bacteria the contribution of microbes to body lysine was estimated at 23 %, with 97 % of this arising through caecotrophy. Absorption of microbial lysine through caecotrophy was 119 (se 4.0) mg/d, compared with 406 (se 1.8) mg/d available from the diet. This study confirms the importance of caecotrophy in rabbit nutrition (15 % of total protein intake).

Difference in rates of net portal absorption between crystalline and protein-bound lysine and threonine in growing pigs fed once daily1

Net portal absorption of AA during the 6-h postprandial period was measured in eight gilts (48.5 ± 1.6 kg BW) in a crossover design. The pigs had chronic catheters placed in the portal vein, carotid artery, and ileal vein, and were trained to consume 1.2 kg of a standard grower diet once daily. Blood samples were taken every 30 min for 4 h and then hourly until 6 h after feeding. The first set of blood samples was taken after pigs were fed a meal of the test 16% CP corn–soybean meal diet (16% CP) or the test 12% CP corn–soybean meal diet supplemented with crystalline lysine, threonine, and tryptophan (12% CP + AA) to equal the three AA levels in the 16% CP diet. Pigs were then fed the standard diet for 2 d. Following that, blood samples were again taken after the pigs were fed a meal of the test diet that was not given to them at the first sampling period. Net portal AA absorption was calculated by multiplying porto-arterial plasma AA concentration difference by portal vein plasma flow rate (PVPF), estimated by an indicator-dilution technique employing p-aminohippuric acid as the indicator infused into the ileal vein. Plasma concentrations of lysine and threonine of pigs were affected by the diet × time interaction (P < 0.01). Portal and arterial plasma lysine and threonine concentrations in pigs attained the maximal level by 1 h postprandial when the 12% CP + AA diet was fed, but reached the peak level at 2.5 h postprandial when the 16% CP diet was given. The PVPF of pigs over the 6 h postprandial was less (P < 0.01) when the 12% CP + AA diet was given than when the 16% CP diet was fed. Net portal absorptions of lysine and threonine also were affected (P < 0.05) by time × diet interaction. The peak portal absorption of both lysine and threonine in pigs appeared at 0.5 h postprandial when the 12% CP + AA diet was given, but at 2.5 h postprandial with the feeding of the 16% CP diet. The early appearance of peak portal absorption of lysine and threonine from feeding the 12% CP + AA compared with the 16% CP diet indicates that crystalline lysine and threonine are absorbed more rapidly than protein-bound lysine and threonine in pigs fed once daily.

Difference in rates of net portal absorption between crystalline and protein-bound lysine and threonine in growing pigs fed once daily.

Net portal absorption of AA during the 6-h postprandial period was measured in eight gilts (48.5 +/- 1.6 kg BW) in a crossover design. The pigs had chronic catheters placed in the portal vein, carotid artery, and ileal vein, and were trained to consume 1.2 kg of a standard grower diet once daily. Blood samples were taken every 30 min for 4 h and then hourly until 6 h after feeding. The first set of blood samples was taken after pigs were fed a meal of the test 16% CP corn-soybean meal diet (16% CP) or the test 12% CP corn-soybean meal diet supplemented with crystalline lysine, threonine, and tryptophan (12% CP + AA) to equal the three AA levels in the 16% CP diet. Pigs were then fed the standard diet for 2 d. Following that, blood samples were again taken after the pigs were fed a meal of the test diet that was not given to them at the first sampling period. Net portal AA absorption was calculated by multiplying porto-arterial plasma AA concentration difference by portal vein plasma flow rate (PVPF), estimated by an indicator-dilution technique employing p-aminohippuric acid as the indicator infused into the ileal vein. Plasma concentrations of lysine and threonine of pigs were affected by the diet x time interaction (P < 0.01). Portal and arterial plasma lysine and threonine concentrations in pigs attained the maximal level by 1 h postprandial when the 12% CP + AA diet was fed, but reached the peak level at 2.5 h postprandial when the 16% CP diet was given. The PVPF of pigs over the 6 h postprandial was less (P < 0.01) when the 12% CP + AA diet was given than when the 16% CP diet was fed. Net portal absorptions of lysine and threonine also were affected (P < 0.05) by time x diet interaction. The peak portal absorption of both lysine and threonine in pigs appeared at 0.5 h postprandial when the 12% CP + AA diet was given, but at 2.5 h postprandial with the feeding of the 16% CP diet. The early appearance of peak portal absorption of lysine and threonine from feeding the 12% CP + AA compared with the 16% CP diet indicates that crystalline lysine and threonine are absorbed more rapidly than protein-bound lysine and threonine in pigs fed once daily.

Parenteral nutrition results in impaired lactose digestion and hexose absorption when enteral feeding is initiated in infant pigs

Preterm infants often receive total parenteral nutrition (TPN) before enteral feeding. Although TPN has been linked to mucosal atrophy, its effects on intestinal digestion, absorption, and metabolism are unknown. Our aim was to determine the effects of TPN on rates of intestinal nutrient absorption and metabolism in infant pigs after initiation of enteral feeding. Piglets were surgically implanted with catheters in the carotid artery, jugular vein, portal vein, and duodenum; an ultrasonic blood flow probe was inserted in the portal vein. Piglets were given TPN (TPN group) or enterally fed formula (enteral group) for 6 d. On day 7, both groups were enterally fed a milk-based formula, and the net portal absorption and metabolism of enteral [(2)H]glucose and [(13)C]leucine were measured. After enteral feeding began, portal blood flow increased by 27% and 41% above the basal rate in the enteral and TPN groups, respectively; oxygen consumption remained lower in the TPN group. During enteral feeding, the net portal absorption of glucose was lower in the TPN group and that of galactose was not significantly different between the groups; lactate release was higher in the TPN group. Portal absorption accounted for only approximately 37% of galactose intake in both groups. The TPN group had lower net portal absorption of arginine, lysine, threonine, and glycine. The portal absorption of dietary leucine was not significantly different between the groups; the arterial utilization and oxidation of leucine were significantly lower in the TPN group. Short-term TPN results in decreased lactose digestion and hexose absorption and increased intestinal utilization of key essential amino acids when enteral feeding is initiated in piglets.

Oral supplementation corrects plasma lysine concentrations in lysinuric protein intolerance

In lysinuric protein intolerance (LPI), intestinal absorption and renal tubular reabsorption of arginine, ornithine, and lysine are impaired due to a defective cationic amino acid transporter. Deficiency of arginine and ornithine restricts the function of the urea cycle, leading to hyperammonemia after protein load, and to strong protein aversion. Mealtime supplements of citrulline, another urea cycle intermediate that uses other transport mechanisms, prevent postprandial hyperammonemia and improve protein tolerance. Deficiency of lysine, an essential amino acid, most probably also contributes to the symptoms of LPI. We investigated possibilities to improve the availability of lysine for tissues by increasing plasma lysine concentration. Six patients with LPI were started on short-term oral lysine supplementation that was administered with their regular citrulline doses and standard low-protein meals. L-Lysine in consecutive doses of 0.55 and 1.1 mmol/kg caused profuse diarrhea in first 3 patients. To avoid gastrointestinal side effects, the 3 other patients were started on smaller lysine supplements of only 0.05 mmol/kg per dose, given 3 times daily for 3 days. All pre- and postprandial plasma lysine concentrations remained within normal range in 2 of the 3 patients studied. Even after the larger doses, no significant effects on the urea cycle were seen. We conclude that low-dose oral lysine supplementation normalizes plasma lysine concentration in patients with LPI, and is safe and well tolerated at least in short-term use.

Lysine synthesized by the gastrointestinal microflora of pigs is absorbed, mostly in the small intestine

This study used a digesta transfer protocol to determine the site of absorption of lysine synthesized by the gastrointestinal microflora of pigs. Eight pigs were used, four with reentrant cannulas in the terminal ileum, two with simple T cannulas in the terminal ileum, and two intact. All pigs were given, for 5 days, the same low-protein diet that included fermentable carbohydrates. The diet of two pigs with reentrant cannulas (donor) and of the two intact (control) pigs was supplemented with (15)NH(4)Cl. The two other pigs with reentrant cannulas (acceptor pigs) and those with simple cannulas (used to supply unlabeled digesta) were given the same diet but unlabeled NH(4)Cl. Ileal digesta were collected continuously from all of the reentrant cannulas and kept on ice. All digesta from each donor pig were reheated and returned to the distal cannula of its companion acceptor, whose ileal digesta were discarded. Unlabeled ileal digesta from the pigs with simple cannulas were instilled into the distal cannulas of the donor pigs. At the end of the experiment, the average (15)N enrichment in the plasma free lysine of control pigs was 0.0407 atom % excess (APE); that of donor pigs was 0.0322 APE (79% of controls), whereas that of acceptor pigs was only 0.0096 APE (24% of controls). Due to nitrogen recycling, acceptor pigs had labeled lysine in the digesta of the stomach and small intestine, and donor pigs had labeled lysine in the digesta of the large intestine. If account is taken of the higher (15)N enrichment of microbial lysine in the large compared with the small intestine, it can be estimated that >90% of the absorption of microbial lysine took place in the small intestine.

Coexpression of the soybean vegetative storage protein beta subunit (S-VSPbeta) either with the bacterial feedback-insensitive dihydrodipicolinate synthase or with S-VSPalpha stabilizes the S-VSPbeta transgene protein and enhances lysine production in transgenic tobacco plants.

Soybean vegetative storage proteins (S-VSPs) are lysine-rich leaf proteins, originally found to accumulate to high levels in depodded soybean plants. In the present study, we overexpressed S-VSPbeta, the ruminant stable subunit of the S-VSP genes, in transgenic tobacco plants. The S-VSPbeta protein accumulated in all organs studied, but its level declined drastically with leaf age. This instability of S-VSPbeta could be overcome either by elevating free lysine levels or by coexpressing S-VSPbeta with S-VSPbeta. High levels of rumen-stable, lysine-rich proteins is expected to improve absorption of lysine by ruminants. Furthermore, the expression of S-VSPs in heterologous plants led to a significant increase in total soluble lysine, suggesting that these proteins may also permit better assimilation of lysine by humans and monogastric animals.

Contribution of intestinal microbial lysine to lysine homeostasis is reduced in minipigs fed a wheat gluten–based diet

We previously reported microbial lysine contribution to plasma lysine homeostasis in humans with an adequate lysine intake. We sought to explore whether the low lysine intake from a wheat gluten-based diet is balanced by enhanced microbial lysine contribution in a pig model. Twenty miniature pigs (minipigs) fitted with ileo-ileal cannulas were fed 2 wheat gluten-based diets. One diet provided 2.7 g lysine/kg diet (WG diet) and one diet was supplemented with crystalline lysine to provide 6.6 g lysine/kg diet (WG+Lys diet). Both diets were fed for 10 or 100 d (n = 5 per group): 10WG+Lys, 10WG, 100WG+Lys, and 100WG diets. Ileal microbial lysine, which we considered to be the precursor pool for absorption, was labeled by oral administration of (15)NH(4)Cl for the final 10 d. On days 10 and 100, a 10-h fast-fed tracer protocol with [1-(13)C]lysine was performed. Lysine rates of appearance decreased by 25% with the WG diet in the fed state but increased by 50% with the WG+Lys diet in the fasted state (P < 0.05). Daily gross microbial lysine contribution was lower (P < 0.05) with the WG diet (205.3 micro mol. kg(-) (1). d(-)(1)) than with the WG+Lys diet (370.7 micro mol. kg(-) (1). d(-)(1)), irrespective of the adaptation period and was similar to the ileal lysine loss with the WG diet. In the WG groups, incorporation of microbial lysine increased in the duodenum and liver (P < 0.05) but not in whole-body and muscle proteins. Minipigs fed the WG diet did not adapt by showing an enhanced absorption of microbial lysine to the extrasplanchnic tissues, presumably because microbial lysine continues to be used for splanchnic protein synthesis.

Absorption of leucine, alanine and lysine from the rumen.

The absorption of three amino acids (leucine, alanine and lysine) from the washed, closed rumen was studied in a short-term (75 min) experiment in situ. The concentration of leucine and alanine did not change in the rumen during the experiment, while that of lysine continuously decreased, and 40% of the total lysine placed in the rumen was absorbed during the experimental period. The rate of absorption decreased in proportion to the fall of amino acid concentration.

Absorption of leucine, alanine and lysine from the rumen

Absorption of leucine, alanine and lysine from the rumen

Availability of intestinal microbial lysine for whole body lysine homeostasis in human subjects.

We have investigated whether there is a net contribution of lysine synthesized de novo by the gastrointestinal microflora to lysine homeostasis in six adults. On two separate occasions an adequate diet was given for a total of 11 days, and a 24-h (12-h fast, 12-h fed) tracer protocol was performed on the last day, in which lysine turnover, oxidation, and splanchnic uptake were measured on the basis of intravenous and oral administration of L-[1-(13)C]lysine and L-[6,6-(2)H(2)]lysine, respectively. [(15)N(2)]urea or (15)NH(4)Cl was ingested daily over the last 6 days to label microbial protein. In addition, seven ileostomates were studied with (15)NH(4)Cl. [(15)N]lysine enrichment in fecal and ileal microbial protein, as precursor for microbial lysine absorption, and in plasma free lysine was measured by gas chromatography-combustion-isotope ratio mass spectrometry. Differences in plasma [(13)C]- and [(2)H(2)]lysine enrichments during the 12-h fed period were observed between the two (15)N tracer studies, although the reason is unclear, and possibly unrelated to the tracer form per se. In the normal adults, after (15)NH(4)Cl and [(15)N(2)]urea intake, respectively, lysine derived from fecal microbial protein accounted for 5 and 9% of the appearance rate of plasma lysine. With ileal microbial lysine enrichment, the contribution of microbial lysine to plasma lysine appearance was 44%. This amounts to a gross microbial lysine contribution to whole body plasma lysine turnover of between 11 and 130 mg. kg(-1). day(-1), depending on the [(15)N]lysine precursor used. However, insofar as microbial amino acid synthesis is accompanied by microbial breakdown of endogenous amino acids or their oxidation by intestinal tissues, this may not reflect a net increase in lysine absorption. Thus we cannot reliably estimate the quantitative contribution of microbial lysine to host lysine homeostasis with the present paradigm. However, the results confirm the significant presence of lysine of microbial origin in the plasma free lysine pool.

Incorporation of urea nitrogen into fecal protein and plasma protein amino acids in elderly human volunteers after ingestion of lactic acid bacteria.

Health effects of fermented milks have been associated with the metabolic activity of lactic acid bacteria in the gastrointestinal tract. It has been proposed that an increased excretion of urea nitrogen via microbial protein may decrease the workload on kidneys and liver. Therefore, a study was carried out in healthy elderly human subjects to investigate the incorporation of [15N2]urea nitrogen into plasma and fecal proteins and amino acids. Over a period of 10 d 13 healthy elderly subjects ingested daily a freeze-dried microbial preparation which contained different genera of lactic acid bacteria and is used to produce fermented milk products. One of the strains was originally isolated from stool samples of elderly people from the Caucasus region (Lactobacillus plantarum). No stimulation of fecal protein-nitrogen excretion and no increase in 15N-abundances in fecal protein was measured following the administration of the viable microbial preparation and a [15N2]urea bolus. Tentatively, it was concluded that this may have been caused by the inability of the microbial culture to survive the gastro-intestinal passage and (or) by the absence of additional fermentable carbohydrates in the diet as energy source for bacterial protein synthesis in the large intestine. However, using a highly sensitive GC-C-IRMS method we observed a significant incorporation of 15N into plasma protein amino acids. 15N-Enrichments in single amino acids were found according to their participation in transamination reactions. The slight enrichment of lysine which is not transaminated in mammalian tissues may indicate a microbial synthesis and absorption of bacterial lysine.

Effect of feeding clinoptilolite (zeolite) on the performance of three strains of laying hens

1. One hundred and twenty 16‐week‐old single combed pullets of three strains were fed on a diet containing 135 g protein/kg with or without 50 g clinoptilolite/kg in a trial with 20 hens per treatment. Sterile river sand replaced clinoptilolite in the control diet in order to keep the diets isoenergetic. The hens were individually caged in a naturally ventilated laying house and fed one of the two diets for ten 28‐d periods. 2. Significant dietary effects of feeding clinoptilolite were observed with number of eggs laid per hen, shell thickness, efficiency of food utilisation and droppings moisture content. No significant dietary effects between treatments were observed with body weight, age at first egg, egg weight, Haugh units, food intake/hen and rate of amino acid absorption of radioactive lysine and methionine into the bloodstream. Significant differences between strains were observed with regard to all parameters except food intake/hen. There were no significant strain × clinoptilolite interactions.

Na+-independent transport of bipolar and cationic amino acids across the luminal membrane of the small intestine.

The role of sodium in transport of bipolar and cationic amino acids and their interactions were examined in vitro by measuring unidirectional influx across the brush-border membrane of intact rat jejunal and rabbit ileal epithelia. The chloride-dependent and beta-alanine inhibitable B(0,+) present in rabbit ileum was blocked by combining inhibition by beta-alanine with Na(+)- or Cl(-)-free conditions. Under these conditions, lysine influx across the brush-border membrane is Na+ independent. All Na+-independent influx of cationic and bipolar amino acids is by a system b(0,+) equivalent in the brush-border membrane of both species, where a system y+ is not present. System b(0,+) is shown to be a potent exchanger of intracellular leucine for extracellular lysine and of intracellular lysine for extracellular leucine. The model used to explain leucine stimulation of mucosa to serosa lysine transport can explain Na+ dependence of net lysine absorption. On the assumption that b(0,+) in situ, like the transporter induced by retroperitoneal brown adipose tissue in Xenopus laevi oocytes, acts as an obligatory exchanger, this model can also explain the effects of lysine on short-circuit current and net transport of sodium and the effect on transport capacity by preincubation at Na+-free conditions.

Microbial amino acid synthesis and utilization in rats: incorporation of 15N from 15NH4Cl into lysine in the tissues of germ-free and conventional rats.

The absorption of lysine synthesised by the gastrointestinal microflora was estimated by comparing the 15N incorporated into body lysine in four germ-free (15N-GF) and four conventional (15N-CV) rats. They were fed for 10 d on a protein-free diet containing fermentable carbohydrates and 15NH4Cl; another four conventional rats (control), fed on the same diet but with unlabelled NH4Cl, were used to estimate the natural abundance of 15N. The eviscerated carcass of each rat was homogenized and a sample hydrolysed. Lysine was isolated by ion-exchange chromatography and its 15N enrichment was measured by isotoperatio mass spectrometry. The 15N-CV rats significantly incorporated 15N into their body lysine. The 15N-GF rats had a statistically significant, although small, incorporation of 15N into their body lysine, probably arising from a measurement artifact. It was concluded, therefore, that all [15N]lysine was of microbial origin. The total lysine content in the body and the 15N enrichment of lysine in the microbial fraction of the faeces of the 15N-CV rats were also determined. The amount of microbial lysine absorbed by the 15N-CV rats was estimated by dividing the total amount of [15N]lysine in the body by the enrichment of microbial lysine. It was estimated that the daily absorption of microbial lysine by the conventional rats was 21.3 (SE 2.04) mg/kg body weight0.75.

Microbial amino acid synthesis and utilization in rats: the role of coprophagy.

Four rats were housed in cages with mesh floors; another four rats were housed in tubular anticoprophagy cages, in which they could not turn round to reach their own faeces. Both groups were fed for 6 d on a low-protein diet containing fermentable carbohydrates and 15NH4Cl. At the end of the experiment the rats were killed and their carcasses were homogenized, lysine was isolated by ion-exchange chromatography and its 15N enrichment measured by isotope-ratio mass spectrometry. The 15N enrichment in the lysine of the microbial fraction of faeces and the total amount of lysine in the body were also determined in order to estimate the amount of microbial lysine absorbed. The 15N enrichment in body lysine of non-coprophagic rats was not different from that previously measured in rats given unlabelled NH4Cl, but in coprophagic rats it was significantly higher. The daily absorption of microbial lysine by the coprophagic rats accounted for 20.7 (SE 2.55) mg/kg body weight0-75, but was only 0.5 (SE 1.04) mg/kg body weight0-75 for the non-coprophagic rats. This value was not significantly different from zero. The utilization of microbial amino acids via coprophagy resulted in a higher weight gain (adjusted for intake) in the coprophagic group (15.5 g/6 d) than in the non-coprophagic rats (3.1 g/6 d). It was concluded that, in rats, the utilization of microbial lysine occurred exclusively via coprophagy.

Absorption of Lysine and Deoxyketosyllysine in an Early-Maillard Browned Casein by the Growing Pig

The aim was to determine the small intestinal uptake in the pig of unaltered (unreacted) lysine in a heat-damaged glucose/casein mixture, containing high concentrations of the early-Maillard compound, deoxyfructosyllysine. Diets containing a heated glucose/casein mixture, where approximately one-third of the original lysine was in the form of deoxyfructosyllysine, and an unheated glucose/casein mixture were each fed to four 10 kg live weight pigs. Chromic oxide was used as an indigestible marker, and digesta were sampled at slaughter, from the terminal ileum. The apparent ileal digestibility of unaltered lysine in the heated glucose/casein was less than unity (59 ± 2.3%, mean ± SE). Gel chromatography of digesta (heated glucose/casein) showed a 430 Da, deoxyfructosyllysine-containing peak, suggesting the presence of deoxyfructosyllysine-containing limit peptides. The FDNB reactive lysine method does not allow accurate assessment of lysine availability in heated proteins, due to incomplete digestion and ab...

Demonstration and characterization of a transport system capable of lysine and leucine absorption that is encoded for in porcine jejunal epithelium by expression of mRNA in Xenopus laevis oocytes.

Defolliculated Xenopus laevis oocytes were injected with size-fractionated poly(A)+ RNA (RNA) isolated from the jejunal epithelium of growing pigs (average BW 33.8 kg) to identify proteins capable of Na+ -independent amino acid transport. The ability of oocytes to absorb L-lysine (lysine) or L-leucine (leucine) from Na+- free media was quantified in oocytes after injection of RNA fractions or water. Specific RNA fractions were identified that induced saturable uptake of lysine (Kt = 52 microM) and leucine (Kt = 97 microM), whereas endogenous oocyte uptake was not saturable. Induced uptake of .05 mM lysine by oocytes was inhibited (P < .05) 68.1% by 5 mM leucine and 38.9% by .2 mM L-cystine (cystine). Induced uptake of .05 mM leucine was inhibited (P < .05) 83.1% by 5 mM lysine and 23.2% by .2 mM cystine. Although not significant (P > .05), 5 mM L-glutamate (glutamate) quantitatively stimulated the induced uptake of .05 mM lysine by 18.8% and the induced uptake of .05 mM leucine by 60%. To identify mRNA species responsible for this bo,+ transporter-like activity, oocytes were co-injected with the RNA fractions and degenerate DNA oligomers complementary (antisense) to the cloned human kidney bo,+ amino acid transporter, or (as a negative control) with a DNA oligomer complementary to the rabbit intestinal Na+/glucose cotransporter, or with water. Only those oocytes injected with two specific RNA fractions and the antisense DNA oligomer complementary to the bo,+ transporter displayed reduced (P < .05) uptake of lysine (45.7, 55.4%) and leucine (44.1, 65.9%). These results indicate that messenger RNA encoding for a protein capable of stimulating the competitive absorption of lysine and leucine is expressed by the jejunal epithelia of growing pigs.

Absorption of lysine and methionine from the proximal colon of the piglet

The present study aimed to determine whether lysine and/or methionine are absorbed in nutritionally significant amounts from the proximal colon of milk-formula-fed piglets (15-32 d old; 2.0-7.4 kg liveweight). Piglets, surgically prepared with simple catheters which allowed infusion into the proximal colon, were randomly allocated to one of two milk-formula diets which were either 40% deficient in lysine (L-diet) or 60% deficient in methionine and 40% deficient in cysteine (S-diet), yet balanced for all other amino acids. The piglets were individually bottle-fed the milk-formula diets seven times daily at 2 h intervals between 08.00 and 20.00 hours. Physiological saline (9 g NaCl/l) or an isotonic solution containing the deficient amino acid was infused via the catheter at each feeding. The experimental procedure followed a cross-over design. Total daily excretions of urinary urea and total N were determined. There were no significant differences (P > 0.05) in urinary N metabolite excretion for piglets infused with amino acids compared with those infused with saline. Lysine and methionine do not appear to be absorbed in nutritionally significant amounts from the proximal colon of the milk-fed piglet.

Effects of a supply of raw or extruded white lupin seeds on protein digestion and amino acid absorption in dairy cows.

Four cannulated, lactating cows were used to determine the effects of extruding white lupin seeds (WLS) on intraruminal CP degradation and absorption of AA from the small intestine. Raw lupin seeds (RWLS) and extruded lupin seeds (EWLS) were fed in diets containing 15.5% CP and composed of 22.4% WLS, 55.9% corn silage, 10.1% maize grain, and 10.6% Italian ryegrass on a DM basis; WLS provided approximately 50% of the total dietary CP. Spot samples of digesta were collected from the proximal duodenum and terminal ileum during 72 h. Chromium EDTA, YbCl3, and purines were used as liquid, particulate, and bacterial markers, respectively. Because of the extensive ruminal degradation of dietary N with the RWLS diet compared with the EWLS diet (64.2 vs 38.8%), less total AA flowed to the duodenum (1,748 vs 2,347 g/d), and because of the decrease of availability (67.2 vs 79.0% of entering), absorption from the small intestine was lowest with this diet (1,175 vs 1,855 g/d). The apparent digestion of individual AA in the small intestine (percentage entering) ranged from 46.5 to 88.4 when cows consumed RWLS and from 58.9 to 94.4 when they were fed the EWLS diet. Among the diets, apparent absorption of histidine, lysine, glycine, and serine were higher than those of other AA; also, valine, alanine, and proline showed intestinal absorptions that were somewhat lower than those of the remainder of the AA.