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PubMedDate not supplied

Enteral glutamine administration prevents the decrease in cell energy charge potential produced in ileum after a skin burn in the rat.

A skin burn produces a decrease in cell energy charge potential (ECP), a marker of cell function, in the liver and other organs. The process appears to be oxidant induced because reduced glutathione (GSH) appears to be protective. The gut mucosal barrier is also known to be altered after burns and appears to be improved by glutamine, which is a source of energy and GSH production. Neither the relationship between the gut barrier change and the ECP of the gut barrier nor the mechanism of glutamine protection has been defined. The effect of a 20% total body surface area, full-thickness burn in a rat on ECP and GSH content in the ileum and the liver and the effect of oral glutamine (1 g/kg/d) on any changes were studied. Three groups of rats (14 rats per group) were studied: a control group, a group with burns alone, and a group with burns that were given glutamine. Half of the rats were killed 1 day after the burn, and the other half were killed 6 days after the burn. ECP did not decrease 1 day after the burn, but 6 days after the burn, ECP decreased from a control of 0.53+/-0.06 to 0.41+/-0.01 in the liver and from 0.64+/-0.04 to 0.29+/-0.04 in the ileum. In the ileum, glutamine prevented the decrease of the ECP (which increased to 0.58+/-.03), but in the liver, glutamine did not alter the ECP (which remained at 0.42+/-0.05). The GSH content was unchanged after the burn injury in both organs compared with the value before the burn injury. It can be concluded that a delayed decrease in ECP in the ileum occurs after a burn injury. Orally administered glutamine prevents the decrease in ECP, probably by providing cell energy rather than by increasing gut GSH (antioxidant) activity.

Administration, Oral↗
PubMed1975

Glutamine transport and metabolism by mitochondria from dog renal cortex. General properties and response to acidosis and alkalosis.

Mitochondria from dog renal cortex were incubated with L-[14Cglutamine. Glutamate metabolism was prevented by inhibitors so that glutamate accumulated either in the mitochondrial matrix space or in the medium. The formation and accumuation of glutamate formed from glutamine and the distribution of glutamine in the mitochondrial fluid spaces were studied. In the matrix space glutamate rapidly reaches levels over 5 times that of glutamine in the medium. A more gradual accumulation occurs in the medium as glutamate is transported out of the mitochondria. Addition of an energy source such as succinate to the medium accelerates glutamate formation. A Km of 0.6 mM appears to govern the reaction at low concentrations of glutamine; at about 4 mM an abrupt change kinetics occurs with a Km of 5 mM above that level. Both NH4+ and glutamate inhibit glutamine metabolism and phosphate stimulates it, but little effect glutamate or phosphate occurs at low levels of these substances. The pH optimum of the reaction is between 7.4 and 7.8. Mersalyl and p-chloromercuribenzoate strongly inhibit glutamate formation; N-ethylmaleimide and bromcresol green have weaker inhibitory actions, and borate increases the reaction rate. In the presence of mersalyl, glutamine is striclly confined to the outer space of mitochondria and none is detectable in the matrix space. Similarly at ) degrees glutamine is confined to the simultaneously determined sucrose or mannitol spaces...

Acidosis↗
PubMed1976

Avian mitochondrial glutamine metabolism.

Intact avian liver mitochondria were shown to synthesize glutamine from glutamate in the absence of exogenous ATP and ammonia. With L-[U-14C]glutamate as the substrate, there was an approximate 1:1 stoichiometry between glutamate deaminated (as measured by the release of 14CO2 due to alpha-keto-[14C]glutarate oxidation) and glutamate amidated. With L-[15N]glutamate as the substrate, the isolated glutamine was shown by low and high resolution mass spectrometry of its phenylisothiocyanate derivative to contain 15N in both the alpha-amino and amide groups. Thus, for each mole of glutamate taken up, approximately 0.5 mol is deaminated and the other 0.5 mol serves as a substrate for glutamine synthetase previously localized in these mitochondria (Vorhaben, J. E., and Campbell, J. W. (1972) J. Biol. Chem. 247,2763). The permeability of L-glutamine to intact avian liver mitochondria was studied by a rapid centrifugation technique. Efflux as well as influx of L-glutamine were both rapid and appeared to occur by a passive, energy-independent process. These results indicate that the mitochondrial glutamine synthetase present in uricotelic species represents the primary ammonia detoxication reaction in that ammonia released intramitochondrially during amino acid catabolism is converted to glutamine for efflux to the cytosol where it may serve as a substrate for purine (uric acid) biosynthesis.

Animals↗
PubMed1976

Alanine and glutamine synthesis and release from skeletal muscle. I. Glycolysis and amino acid release.

The synthesis and release of alanine and glutamine were investigated with an intact rat epitrochlaris muscle preparation. This preparation will maintain on incubation for up to 6 hours, tissue levels of phosphocreatine, ATP, ADP, lactate, and pyruvate closely approximating those values observed in gastrocnemius muscles freeze-clamped in vivo. The epitrochlaris preparation releases amino acids in the same relative proportions and amounts as a perfused rat hindquarter preparation and human skeletal muscle. Since amino acids were released during incubation without observable changes in tissue amino acids levels, rates of alanine and glutamine release closely approximate net amino acid synthesis. Large increases in either glucose uptake or glycolysis in muscle were not accompanied by changes in either alanine or glutamine synthesis. Insulin increased muscle glucose uptake 4-fold, but was without effect on alanine and glutamine release. Inhibition of glycolysis by iodacetate did not decrease the rate of alanine synthesis. The rates of alanine and glutamine synthesis and release from muscle decreased significantly during prolonged incubation despite a constant rate of glucose uptake and pyruvate production. Alanine synthesis and release were decreased by aminooxyacetic acid, an inhibitor of alanine aminotransferase. This inhibition was accompanied by a compensatory increase in the release of other amino acids, such as aspartate, an amino acid which was not otherwise released in appreciable quantities by muscle. The release of alanine, pyruvate, glutamate, and glutamine were observed to be interrelated events, reflecting a probable near-equilibrium state of alanine aminotransferase in skeletal muscle. It is concluded that glucose metabolism and amino acid release are functionally independent processes in skeletal muscle. Alanine release reflects the de novo synthesis of the amino acid and does not arise from the selective proteolysis of an alanine-rich storage protein. It appears that the rate of alanine and glutamine synthesis in skeletal muscle is dependent upon the transformation and metabolism of amino acid precursors.

Adenine Nucleotides↗
PubMed2002

[The effects of glutamine dipeptide on the improvement of endotoxemia in severely burned patients].

OBJECTIVE: To explore the influence of glutamine dipeptide on the plasma endotoxin levels in severely burned patients. METHODS: Thirty burned patients with TBSA of 30 - 70% and III degree burn area more than 20% were randomly divided into control (C) and study (S) groups. Glutamine dipeptide powder in dose of 0.5 g/kg/day was given orally in bolus to those patients in S group during 1 - 12 postburn days (PBDs). The plasma levels of glutamine were determined during 1 - 12 PBDs. Simultaneously, the plasma endotoxin level was detected on 1, 3, 6 and 12 PBDs. The wound healing rate at 30 PBD and total hospital stay days were recorded. RESULTS: The plasma glutamine levels at 1 PBD in C and S groups were obviously lower than normal level (659.5 +/- 35 micromol/L), but there was no difference between these two groups (P > 0.05). The plasma glutamine levels in C group was much lower than that in S group at 12 PBD (P < 0.05). The plasma endotoxin concentration on 1 PBD in these two groups increased evidently compared with the normal value (P < 0.05), and there was no difference between the two groups (P > 0.05). The plasma endotoxin level in S group was much lower than that in C group on 3 PBD (P < 0.05). As for the wound healing rate at 30 PBD, it was markedly higher in S group than that in C group (91% vs 85%). On the other hand, the hospital stay days in S group were evidently lower than that in C group (52 vs 67). CONCLUSION: Oral intake of glutamine dipeptide in burn patients could be beneficial to the maintenance of the plasma concentration of glutamine and in decreasing plasma endotoxin level. It would also enhance the wound healing rate at 30 PBD and shorten the hospital stay days.

Adolescent↗
PubMed2004

[Effects of glutamine granules on protein metabolism in trauma patients].

OBJECTIVE: To evaluate the effect of glutamine granules on protein metabolism in severe burns and trauma patients. METHODS: 120 patients with severe burns, multiple trauma and post operation who met the requirements of the protocol joined this double-blind randomized controlled, multi-center clinical trail. Patients were randomly divided into two groups: placebo control group (P group, 60 patients) and glutamine granules treatment group (GLN group, 60 patients). There was isonitrogenous and isocaloric intake in both groups, GLN and P group patents had been given glutamine granules or placebo (glycine) at 0.5 g.kg(-1).d(-1) for 7 days, respectively. The level of plasma glutamine, protein and urine nitrogen exclude were determined, wound healing rate of burn area and hospital stay were recorded, and then observed the complication and side effect. RESULTS: After 7 days of taking glutamine granules orally, plasma GLN concentration was significant higher than that in P group (592.50 +/- 185.23 micro mol/L vs. 407.41 +/- 190.22 micro mol/L) (P < 0.01). Plasma prealbumin and transferrin in GLN group were significant higher than those in P group (P < 0.01), but the concentration of total protein and albumin were no marked changes compare with P group (P > 0.05). The capacity of urine nitrogen exclude in GLN group were significant lower than that in P group. Additional, the wound healing rate was faster and hospital stay days was shorter than P group (P < 0.05), and the occurrence of glutamine granules side effect was seldom. CONCLUSION: Taking glutamine could promote protein synthesis, abate protein decompose, ameliorate wound healing rate and reduce hospital stay obviously.

Adult↗
PubMed2005

[Effects of glutamine granules on immunofunction in trauma patients: a double-blind randomized controlled, multi-center clinical trail with 120 patients].

OBJECTIVE: To evaluate the effect of glutamine granules on immunofunction in severe burns and trauma patients. METHODS: One hundred and twenty patients with severe burns, multiple trauma and post operation who met the requirements of the protocol joined this double-blind randomized controlled, multi-center clinical trail. Patients were randomly divided into two groups: placebo control group (P group, 60 patients) and glutamine granules treatment group (GLN group, 60 patients). There was isonitrogenous and isocaloric intake in both groups. GLN and P group patients had been given glutamine granules or placebo (glycine) at 0.5 g.kg(-1).d(-1) for 7 days, respectively. The level of plasma glutamine and some index of immunofunction were determined, and the complication and side effect were also observed. RESULTS: After 7 days of taking glutamine granules orally, plasma GLN concentration was significantly higher than that in P group [(593 +/- 185) micromol/L vs (407 +/- 190) micromol/L)] (P < 0.01). IL-2 level, CD(4)/CD(8) ratio, PMN swallow ratio in GLN group were significantly higher than those in P group (P < 0.05-0.01), but the concentration of IgG, IgM, C(3)/C(4) were not significantly different when compared with P group (P > 0.05). In addition, the occurrence of side effect in both groups was seldom. CONCLUSION: Taking glutamine granules could increase plasma GLN concentration, enhance body immunofunction, and using glutamine granules is safe.

Administration, Oral↗
PubMed2006

[Early enteral and glutamine enriched enteral feeding ameliorates healing of colonic anastomosis: experimental study].

BACKGROUND: To investigate the effects of postoperative early enteral and glutamine enriched enteral feeding on the healing of experimental colonic anastomosis. METHODS: Forty Wistar-albino rats were equally divided into 4 groups. Colonic transsection and anastomosis situated at the distal left colon was performed on all animals. Animals in groups 1 and 2 received late total enteral nutrition (TEN) and in groups 3 and 4 early TEN. Glutamine was added to TEN protocol in groups 2 and 4. The colonic segment including the anastomosis was excised at the end of the 7th day postoperatively. Bursting pressure of the anastomosis and tissue hydroxyproline levels were determined. RESULTS: Bursting pressure levels were 111.6 and 95.8 centimeters of water (cmH(2)O) in early and late nutrition groups, respectively (p=0.022). Comparison of late TEN groups showed a significant difference in favor of group with glutamine (95.8 vs 138.5 cmH(2)O; p<0.0001). Highest bursting pressures (139 and 138.5 cmH(2)O) were measured in both early and late TEN groups with glutamine. Tissue hydroxyproline level in early TEN group (2440.3 microg) was significantly higher than late TEN group (1509.6 microg; p=0.024). Comparison of late TEN groups showed a considerable but not statistically significant difference (p=0.276) in favor of group with glutamine (1509.6 vs 1981.6 microg). CONCLUSION: Postoperative early TEN significantly ameliorates the resistance of the anastomosis and collagen synthesis. Glutamine enrichment in nutritional protocol decreases and reverses the disadvantages of late TEN regarding the resistance of anastomosis. A similarly positive, albeit weaker, effect of glutamine supplementation is also seen on collagen synthesis.

Anastomosis, Surgical↗
PubMedDate not supplied

Oral glutamine ameliorates chemotherapy-induced changes of intestinal permeability and does not interfere with the antitumor effect of chemotherapy in patients with breast cancer: a prospective randomized trial.

AIMS AND BACKGROUND: Sixty patients with breast cancer were randomly assigned to oral glutamine or placebo pre-neoadjuvant chemotherapy (CEF regimen). METHODS AND STUDY DESIGN: Oral glutamine supplementation was continued for at least 12 days. Patients kept a daily record of diarrhea and stomatitis. The plasma glutamine level, intestinal permeability (lactulose-mannitol test), and tumor size were analyzed. The expression of Ki-67 and PCNA antigens in breast carcinoma was assessed. RESULTS: The plasma glutamine level was significantly higher in the glutamine group than in the placebo group (420.39 +/- 52.39 mmol/L vs 309.76 +/- 42.34 mmol/L, P < 0.05). After one cycle of chemotherapy, the lactulose-mannitol ratio was higher in the placebo group than in the glutamine group (0.0630 +/- 0.0091 vs 0.0471 +/- 0.0094, P < 0.05). No differences were observed in the grades of stomatitis and diarrhea, in the changes in tumor size, and in the expression of Ki-67 and PCNA antigens between the two groups. CONCLUSIONS: Prophylactic oral glutamine could ameliorate the neoadjuvant chemotherapy-induced increase in intestinal permeability, but had no significant positive clinical effect on stomatitis and diarrhea and did not interfere with the antitumor effect of chemotherapy.

Administration, Oral↗
PubMed1990

Glucose and glutamine metabolism in the small intestine of septic rats.

The intestinal metabolism of glucose and glutamine was studied in rats made septic by cecal ligation and puncture technique. Sepsis resulted in negative nitrogen balance and produced increases in the concentrations of blood pyruvate, lactate, alanine, and glutamine, and decreases in those of 3-hydroxybutyrate and acetoacetate. Both plasma insulin and glucagon concentrations were increased by 2.2- and 3.2-fold in septic rats, respectively. Portal-drained visceral blood flow increased in septic rats, and was accompanied by a decrease in the rates of utilization of glutamine and production of lactate, glutamate, and ammonia compared with those rates in sham-operated animals. Enterocytes isolated from septic rats showed decreased rates of glucose and glutamine utilization compared with cells isolated from corresponding controls. The maximal activities of hexokinase, 6-phosphofructokinase, pyruvate kinase, and glutaminase were decreased in intestinal mucosal scrapings of septic rats. It is concluded that a moderate form of sepsis decreases the rates of glucose and glutamine utilization (both in vivo and in vitro) by the epithelial cells of the small intestine. This may be caused by changes in the maximal activities of key enzymes in the pathways of glucose and glutamine metabolism in these cells as a metabolic adaptation to spare glucose and glutamine for use by other tissues.

Animals↗
PubMed1988

The glutamine residues reactive in transglutaminase-catalyzed cross-linking of involucrin.

The protein involucrin, synthesized by human keratinocytes, contains 585 amino acids, largely in the form of 10 amino acid repeats, each containing glutamines in 3 conserved positions. Involucrin is a substrate for the keratinocyte transglutaminase and is labeled by the cosubstrate amine, glycine ethyl ester. Study of tryptic peptides of involucrin shows that a single glutamine (residue 496), located 89 residues from the C-terminal end, is preferentially labeled by the enzyme. Additional glutamine residues become reactive when the molecule is fragmented. The C-terminal end, isolated as a cyanogen bromide fragment of 275 residues, is labeled equally at 2 glutamine residues. The polypeptide containing residues 148 to 280 accepts practically no amine while in intact involucrin but as a free fragment is labeled at multiple glutamine residues. It is concluded that the C-terminal and N-terminal ends of the protein are directive influences in that they suppress the reactivity of a number of glutamine residues in the intact molecule, leaving one glutamine highly preferred by the transglutaminase.

Amino Acid Sequence↗
PubMed1986

Effect of acivicin on glutamine transport by rat renal brush border membrane vesicles.

Acivicin (L-[alpha S,5S]-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid) reversibly and competitively inhibits glutamine transport in rat renal brush border membrane (BBM) vesicles. Acivicin alters the affinity of the low-Km high-affinity glutamine transport system, but has minimal effect on the high-Km low-affinity system. The drug interferes with glutamine transport by a mechanism that does not involve the maintenance of a Na+-chemical gradient as shown by its uniform effect on glutamine uptake rate, regardless of the NaCl gradient imposed (0 to 150 mmol/L). The effect of acivicin on membrane potential was ruled out by the finding that acivicin modified glutamine transport even when the membrane potential was minimized either by substituting Cl- with an impermeant anion, isethionate, or by short-circuiting the membrane potential with carbonyl cyanide p-trifluoromethoxyphenyl hydrazone. In these experiments the activity of the enzyme gamma-glutamyltranspeptidase (gamma-GT), a component of the putative amino acid transport system, was not suppressed because the BBM was not preincubated with acivicin. Acivicin also interferes with the uptake of other solutes tested (alanine, proline, glutamate, and glucose). But with the exception of L-alanine, the transport of these solutes is less sensitive to the inhibitory effect of acivicin than is that of glutamine. Our results indicate that acivicin profoundly affects the metabolism of renal tubular cells by its influence on the metabolite transport systems. Acivicin can reduce renal NH3 production independently of its effect on gamma-GT by interfering directly with renal cellular uptake of glutamine.

Amino Acids↗
PubMed1987

Trypanosoma congolense: differentiation to metacyclic trypanosomes in culture depends on the concentration of glutamine or proline.

The effect of glutamine on the number of metacyclic trypanosomes produced in insect form cultures of Trypanosoma congolense TREU 1457 was investigated. When cultured in the absence of glutamine, trypanosomes did not develop to metacyclic forms. While metacyclics were produced in all cultures maintained with glutamine in the concentration range 2-20 mM, optimum numbers were obtained between 4 and 12 mM glutamine. This pattern was constant in flasks cultured for over two months. The substitution of glutamine by proline in culture medium did not influence the number of metacyclic forms produced. Removal of proline or glutamine from cultures producing metacyclics caused a rapid fall in production of metacyclic forms which could be reversed by re-introduction of either nutrient. Cultures of another stock of T. congolense responded similarly when maintained in different concentrations of glutamine, showing that the effect may be a general one.

Animals↗
PubMedDate not supplied

The role of oxidation in the renal metabolism of glutamine by rat kidney tubules in vitro.

The metabolism of cold and 14C-[U]-glutamine in isolated kidney tubules of normal rats was studied in vitro to establish the relative importance of glucose synthesis and complete oxidation to CO2 for the metabolism of this amino acid in vitro. These metabolic fates were estimated by drawing a complete balance of the nitrogens and of the carbon chains of the extracted glutamine and studying the formation of 14CO2 from 14C-glutamine. It was found that glucose production constitutes the major fate for glutamine metabolism with 1 mM glutamine and that glutamine oxidation constitutes less than 20% of the metabolic fate of the carbon skeleton of this amino acid. With 5 or 10 mM glutamine however, the maximal oxidation to CO2 becomes more important (25%).

Animals↗
PubMed1983

Prominent glutamine oxidation activity in mitochondria of hematopoietic tumors.

Well-coupled mitochondria of hematopoietic tumors were isolated from mouse erythroleukemia and rat chloroma tumors grown in male DBA/2J mice and Long-Evans rats, respectively. We used erythroleukemia and chloroma mitochondria to determine their ability to utilize glutamine as an energy source for adenosine triphosphate formation. Oxypolarographic tests showed the following. (a) Presence of a prominent glutaminase activity in erythroleukemia and chloroma mitochondria is evidenced by their active glutamine-supported respiratory state 3. (b) Glutamine oxidation is mediated through a nicotinamide adenine dinucleotide-linked reaction inhibited by rotenone. (c) Under similar conditions, mitochondria isolated from rabbit bone marrow have shown a feeble glutamine oxidation activity, while in mitochondria from rat liver the activity was not detectable and in those from rat kidney it was prominent as expected. (d) The determination of apparent Km and Vmax values for substrate-supported adenosine triphosphate formation has shown 8- to 10-fold lower Km values for glutamine oxidation as compared to that of glutamate, with virtually the same Vmax for each substrate in each mitochondria. These results clearly show the presence of a high glutamine oxidation activity in erythroleukemia and chloroma mitochondria and suggest that one of the glutamine hydrolysis products in those mitochondria may have an important role in supplying adenosine triphosphate in the corresponding malignant cells.

Adenosine Triphosphate↗
PubMed1984

Glutamine: a major energy source for cultured mammalian cells.

Cultured mammalian cells have two primary mechanisms for obtaining energy necessary for growth: carbohydrate metabolism to lactate and glutamine oxidation to CO2. In tissue culture medium containing both glucose and glutamine, the contribution of glutamine oxidation to the energy requirement ranges between 30 and 50%. As the glucose concentration is decreased, or when glucose is replaced by other carbohydrates, the rate of glutamine oxidation increases and glutamine becomes the sole energy source for cultured cells. The rate of glutamine oxidation is regulated by the presence of glucose. The apparent absolute requirement for glucose or other carbohydrates in tissue culture medium is related to its role in anabolic reactions rather than in energy production. Oxidation of glucose, fatty acids, or ketone bodies does not contribute significantly to the energy needs of cultured mammalian cells. The data also suggest that consideration should be given to glutamine as an important energy source in vivo.

Cell Division↗
PubMed1995

Glutamine transport in isolated human hepatocytes and transformed liver cells.

The transport of L-glutamine was examined in isolated adult and fetal human hepatocytes as well as in the human hepatoma cell lines HepG2 and SK-Hep. In all cells studied, glutamine uptake was at least 85% Na(+)-dependent. Kinetic analysis of the Na(+)-dependent component indicated mediation by a single transporter in three human hepatocyte preparations and in SK-Hep cells, whereas two transporters appeared to be responsible for glutamine uptake in HepG2 cells and in hepatocytes from the liver of one male patient. Amino acid inhibition analysis showed primary mediation by System N in fetal and adult hepatocytes, whereas System ASC was principally responsible for glutamine uptake in transformed cells. Similar to the rat transporter, human System N was pH-sensitive, stereospecific, and responsive to treatment with steroid hormones. Although the human carrier was less tolerant of Li(+)- for Na+ substitution, glutamine transport in primary human hepatocytes was stimulated by treatment with hypotonic buffer (cell swelling), as reported in rat parenchymal cells. In contrast, glutamine transport in hepatoma cells was relatively insensitive to changes in extracellular pH and failed to show enhanced activity in response to hypoosmotic challenge. Collectively, the data suggest that markedly distinct plasma membrane transporters mediate the concentrative uptake of glutamine in normal and transformed human hepatocytes, and that the salient properties of System N have been largely conserved from rat to man.

Adult↗
PubMed1997

Effect of glutamine or glycine containing oral electrolyte solutions on mucosal morphology, clinical and biochemical findings, in calves with viral induced diarrhea.

Twenty-one diarrheic calves were randomly assigned to 1 of 3 oral electrolyte treatments. The treatments were either a conventional oral electrolyte containing glycine (40 mmol/L) as the amino acid, an oral electrolyte in which glutamine (40 mmol/L) replaced glycine or an electrolyte in which high concentrations of glutamine (400 mmol/L) replaced glycine. The calves were monitored while on trial and at the end of the treatment they were euthanized and a necropsy was immediately performed. Calves fed the high glutamine electrolyte had more treatment failures (2/7 versus 0/7 for each of the other 2 treatments). There was a significant effect of type of electrolyte on fecal consistency. Calves fed the glycine containing electrolyte had the most solid feces. Duodenal villus height was significantly affected by the type of electrolyte: values (mean +/- 1 SEM) were 0.61 +/- 0.09, 0.46 +/- 0.05, and 0.59 +/- 0.07 mm for high glutamine, low glutamine and glycine electrolytes respectively. There was no significant difference in small intestinal surface area between groups. High glutamine treated calves had the greatest capacity to absorb xylose from the small intestine but this difference was not statistically significant. Overall, this trial does not suggest that substituting glutamine for glycine in oral electrolyte solutions improves treatment of diarrheic calves or speeds mucosal healing.

Animals↗