• Proceedings of the Korea Society of Poultry Science Conference
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• 2004.11a
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• pp.80-90
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• 2004

Three experiments were performed to test the assumption that imbalanced dietary amino acid mixtures must lead to increased heat production (HP). The first experiment was based on diets formulated to have a wide range of crude protein (CP) concentrations but a fixed concentration of lysine, formulated to be the first-limiting amino acid. In the second (converse) experiment, lysine concentration was varied over a wide range while CP content was kept constant. To prevent the masking of dietary effects by thermoregulatory demands, the third experiment was performed at 30 $^{\circ}C$ with the diets similar to the diets used in the second experiment. The detailed relationships among amino acid balance, nitrogen (N) metabolism and energy (E) metabolism were investigated in a computer-controlled chamber calorimetry system. The results of experiments were compared with the predictions of a computerised simulation model of E metabolism. In experiment 1. with constant lysine and varying CP, there was a 75 % increase in N intake as CP concentration increased. This led to a 150 % increase in N excretion. with no significant change in HP. Simulated HP agreed with the empirically determined results in not showing a trend with dietary CP. In experiment 2, with varying lysine but constant CP, there was a 3-fold difference in daily weight gain between the lowest and highest lysine diets. HP per bird increased significantly with dietary lysine concentration. There was still an effect when HP was adjusted for body weight differences, but it failed to maintain statistical significance. Simulated HP results agreed in showing little effect of varying lysine concentration and growth rate on HP. Based on the results of these two experiments, the third experiment was designed to test the response of birds to dietary lysine in high ambient temperature. In experiment 3 which performed at high ambient temperature (30 $^{\circ}C$), HP per bird increased significantly with dietary lysine content, whether or not adjusted for body-weight. The trend was greater than in the previous experiment (20 $^{\circ}C$).

• Journal of Chest Surgery
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• v.42 no.4
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• pp.409-417
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• 2009

Background: Glutaraldehyde-fixed heterografts are prone to calcification after long-term implantation in human, and this is one of the limiting factors for the longevity of the heterografts used in cardiovascular surgery. The aim of the study was to evaluate the anticalcification effect of an ethanol and amino acids treatment on glutaraldehyde-fixed bovine pericardium. Material and Method: Bovine pericardial tissues were divided into 5 groups. Group 1 consisted of tissues fixed with glutaraldehyde, group 2 consisted of commercially available bovine pericardial valve tissues (Carpentier-Edwards PERIMOUNT), group 3 consisted of glutaraldehyde-fixed tissues treated with ethanol, group 4 consisted of glutaraldehyde-fixed tissues treated with ethanol and L-glutamic acid, and group 5 consisted of glutaraldehyde-fixed tissues treated with ethanol and homocysteic acid. The tissue microstructure was examined by light and electron microscopy. Tissue samples of each group were implanted into rat subcutaneous tissue for 3 $\sim$ 4 months and the calcium contents were measured after harvest. Result: The collagen fibers appeared to be well preserved in all the groups. The calcium contents of groups 2, 3, 4 and 5 (13.46$\pm$11.74, 0.33$\pm$0.02, 0.39$\pm$0.08 and 0.42$\pm$0.06 $\mu$g/mg, respectively) were all significantly lower than that of group 1 (149.97$\pm$28.25 $\mu$g/mg) (p<0.05). The calcium contents of groups 3, 4 and 5 were all significantly lower than that of group 2 (p<0.05). Conclusion: Treatment with ethanol alone or in combination with amino acids (L-glutamic acid or homocysteic acid) strongly prevented the calcification of glutaraldehyde-fixed bovine pericardium.

• Korean Journal of Food Science and Technology
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• v.15 no.2
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• pp.170-176
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• 1983

Starchy single cell protein produced by a starch-utilizing yeast, Sporobolomyces holsaticus FRI Y-5 was analyzed for its composition such as intracellular protein, amino acids, fatty acids, minerals, vitamins and pigments. It was shown that it contained 33.08% of total carbohydrate, 45.63% of crude protein, 20.01% of crude lipid, 3.24% of ash and 4.46% of pigment. Whole cell extracted by cold and hot NaOH method contained 40.89% of soluble protein and the estimated nucleic acid content from crude and soluble protein contents was about 7.6%. The sulphur-containing amino acids, threonine, isoleucine and valine were analyzed to be the limiting amino acids in the starchy SCP, and the protein score was calculated as 89.4. It was shown from its fatty acid analysis that it contained $6.5%\;of\;C_{16:0}$, $2.4%\;of\;C_{18:0}$, $81.9%\;of\;C_{18:1}$, $3.2%\;of\;C_{18:2}$, and $6.0%\;of\;C_{18:3}$. Also it was observed that it contained, per 100 g of dry cell, 365.33mg of Mg and 282.75mg of K more than Fe and Ca. The content of Vit. $B_2$ was 3.7mg per 100 g of dry cell, but niacin was not detected under this experimental condition. The UV-visible scanning result of pigment extract showed that the yeast contained carotenoid and unknown pigments.

• YAKHAK HOEJI
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• v.51 no.2
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• pp.83-87
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• 2007

The effects of ethaverine on serotonin biosynthesis in murine mastocytoma P815 cells were investigated. Ethaverine at 2.5${\sim}$10 ${\mu}$M decreased serotonin content in a concentration-dependent manner. The IC$_{50}$ value of ethaverine was 6.1 ${\mu}$M. Ethaverine at concentrations up to 20 ${\mu}$M was not cytotoxic towards P815 cells. Under these conditions, tryptophan hydroxylase (EC 1.14.16.4; TPH), a rate-limiting enzyme in serotonin biosynthesis, was inhibited by ethaverine in P815 cells (15.3% inhibition at 7.5 ${\mu}$M), however, aromatic L-amino acid decarboxylase (EC 4.1.1.28) was not. These results indicate that ethaverine leads to a decrease in serotonin content by reducing TPH activity in P815 cells.

• Nutritional Sciences
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• v.6 no.4
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• pp.189-194
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• 2003

Most of the ethyl alcohol consumed by humans is oxidized to acetaldehyde in the liver by the cytoplasmic alcohol dehydrogenase (ADH) system. For this ADH-catalyzed oxidation of alcohol, $NAD^+$ is required as the coenzyme and $NAD^+$becomes reduced to NADH. As the $NAD^+$becomes depleted and NADH accumulates, alcohol oxidation is reduced. For continued alcohol oxidation, the accumulated NADH must be quickly reoxidized to $NAD^+$, and it is this reoxidation of NADH to $NAD^+$that is known to be the rate-limiting step in the overall oxidation rate of alcohol The reoxidation of NADH to $NAD^+$is catalyzed by lactate dehydrogenase in the cytoplasm of hepatocytes, with pyruvate being utilized as the substrate. The pyruvate may be supplied from alanine as a result of amino acid metabolism via the urea cycle. Also, glutamine is thought to help with the supply of pyruvate indirectly, and to activate the urea cycle by producing $NH_3$. Thus, in the present study, we have examined the effects of alanine and glutamine on the alcohol oxidation rate. We utilized isolated perfused liver tissue in a system where media containing alanine and glutamine was circulated. Our results showed that when alanine (5.0mM) was added to the glucose-free infusion media, the alcohol oxidation rate was increased by 130%. Furthermore, when both glutamine and alanine were added together to the infusion media, the alcohol oxidation rate increased by as much as 190%, and the rate of urea nitrogen production increased by up to 200%. The addition of glutamine (5.0mM) alone to the infusion media did not accelerate the alcohol oxidation rate. The increases in the rates of alcohol oxidation and urea nitrogen production through the addition of alanine and glutamine indicate that these amino acids have contributed to the enhanced supply of pyruvate through the urea cycle. Based on these results, it is concluded that the dietary supplementation of alanine and glutamine could contribute to increased alcohol detoxification through the urea cycle, by enhancing the supply of pyruvate and $NAD^+$to ensure accelerated rates of alcohol oxidation.

• Molecules and Cells
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• v.28 no.6
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• pp.575-581
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• 2009

Ornithine decarboxylase (ODC) is a rate-limiting enzyme in the biosynthesis of polyamines, which are essential for cell growth, differentiation, and proliferation. This report presents the characterization of an ODC-encoding cDNA (SlitODC) isolated from a moth species, the tobacco cutworm, Spodoptera litura (Lepidoptera); its expression in a polyamine-deficient strain of yeast, S. cerevisiae; and the recovery in polyamine levels and proliferation rate with the introduction of the insect enzyme. SlitODC encodes 448 amino acid residues, 4 amino acids longer than B. mori ODC that has 71% identity, and has a longer C-terminus, consistent with B. mori ODC, than the reported dipteran enzymes. The null mutant yeast strain in the ODC gene, SPE1, showed remarkably depleted polyamine levels; in putrescine, spermidine, and spermine, the levels were > 7, > 1, and > 4%, respectively, of the levels in the wild-type strain. This consequently caused a significant arrest in cell proliferation of > 4% of the wild-type strain in polyamine-free media. The transformed strain, with the substituted SlitODC for the deleted endogenous ODC, grew and proliferated rapidly at even a higher rate than the wild-type strain. Furthermore, its polyamine content was significantly higher than even that in the wild-type strain as well as the spe1-null mutant, particularly with a very continuously enhanced putrescine level, reflecting no inhibition mechanism operating in the putrescine synthesis step by any corresponding insect ODC antizymes to SlitODC in this yeast system.

• Journal of Animal Science and Technology
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• v.48 no.4
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• pp.541-554
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• 2006

Present review is to introduce an omasal sampling technique in rumen proteolysis and to consider some information on the omasal sampling technique with particular emphasis on methodological aspects. Use of the omasal sampling technique provides a new opportunity for accurate estimation of rumen metabolism with overcoming limitations of previous in vivo, in vitro and/or in situ methods. The potential advantages of the present technique compared with post-ruminal sampling techniques include following points; 1) only rumen cannulated animals are required, 2) less endogenous nitrogen (N) is contaminated in omasal digesta and 3) omasal digesta are devoid of exposure to acid peptide hydrolysis occurring in the abomasum. Estimates of soluble non-ammonia N (SNAN) in omasal digesta indicate that the assumptions underlying the in situ method that rapidly degradable N fraction can be degraded at an infinite rate and only insoluble dietary N escapes the rumen may be not valid. Quatitatively higher peptide concentration rather than free amino acid and soluble protein in escapable SNAN suggests that hydrolysis of peptide to amino acid may be the rate-limiting step in rumen proteolysis.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.10
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• pp.1460-1468
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• 2003

An experiment was conducted to quantify the flow of soluble non-ammonia nitrogen (SNAN) in the liquid phase of ruminal (RD) and omasal digesta (OD), and to investigate diurnal pattern in SNAN flow in OD. Five ruminally cannulated Finnish-Ayrshire dairy cows in a $5{\times}5$ Latin square design consumed a basal diet of grass silage and barley grain, and that supplemented with four protein feeds (kg/d DM basis) as follows: skimmed milk powder (2.1), wet distiller' solubles (3.0), untreated rapeseed meal (2.1) and treated rapeseed meal (2.1). Ruminal digesta was sampled using a vacuum pump, whereas OD was collected using an omasal sampling system at 1.0 h interval during a 12 h feeding cycle. Both RD and OD were acidified, centrifuged to remove microbes and precipitated with trichloroacetic acid followed by centrifugation. The SNAN fractions (free amino acid (AA), peptide and soluble protein) in RD and OD were assessed using ninhydrin assay. Free AA, peptide and soluble protein averaged 60.0, 89.4 and 2.1 g/d, respectively, for RD, and 81.8, 121.5 and 2.5 g/d, respectively, for OD. Although free AA flow was relatively high, mean peptide flow was quantitatively the most important fraction of SNAN, indicating that degradation of peptide to AA rather than hydrolysis of soluble protein to peptide or deamination may be the most limiting step in rumen proteolysis. Diurnal pattern in flow of peptide including free AA in OD during a 12 h feeding cycle peaked 1 h post-feeding, decreased by 3 h post-feeding and was relatively constant thereafter. Protein supplementation showed higher flow of peptide including free AA immediately after feeding compared with no supplemented diet. There were no differences among protein supplements in diurnal pattern in flow of peptide including free AA in OD.

• Asian-Australasian Journal of Animal Sciences
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• v.25 no.9
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• pp.1269-1275
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• 2012

An experiment was conducted to study the effect of soluble protein supplements on concentration of soluble non-ammonia nitrogen (SNAN) in the liquid phase of ruminal (RD) and omasal digesta (OD) of Korean native steers, and to investigate diurnal pattern in SNAN concentration in RD and OD. Three ruminally cannulated Korean native steers in a $3{\times}3$ Latin square design consumed a basal diet of rice straw and corn-based concentrate (control), and that supplemented (kg/d DM basis) with intact casein (0.24; IC) or acid hydrolyzed casein (0.46; AHC). Ruminal digesta was sampled using a vacuum pump, whereas OD was collected using an omasal sampling system at 2.0 h intervals after a morning feeding. The SNAN fractions (free amino acid (AA), peptide and soluble protein) in RD and OD were assessed using the ninhydrin assay. Concentrations of free AA and total SNAN in RD were significantly (p<0.05) lower than those in OD. Although free AA concentration was relatively high, mean peptide was quantitatively the most important fraction of total SNAN in both RD and OD, indicating that degradation of peptide to AA rather than hydrolysis of soluble protein to peptide or deamination may be the most limiting step in rumen proteolysis of Korean native steers. Diurnal variation in peptide concentration in OD for the soluble protein supplemented diets during the feeding cycle peaked 2 h post-feeding and decreased thereafter whereas that for the control was relatively constant during the entire feeding cycle. Diurnal variation in peptide concentration was rather similar between RD and OD.

• Asian-Australasian Journal of Animal Sciences
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• v.20 no.8
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• pp.1297-1304
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• 2007

We conducted a series of investigations in order to elucidate role of nutritional status in regulating GLUT expression and energy metabolism in porcine muscle. Firstly, the role of mild undernutrition in regulating muscle GLUT gene expression and function was studied in growing pigs (3 wk of age) on a high (H) or low (L) food intake (H = 2L) at $35^{\circ}C$ or $26^{\circ}C$. Low food intake selectively upregulates GLUT1 and GLUT4 gene expression; mRNA levels were elevated in longissimus dorsi (L. dorsi) and rhomboideus muscles but not in diaphragm or cardiac muscles. Our next step was to determine whether dietary lysine, a major primary limiting amino acid in diets for pigs, affects muscle GLUT4 expression. Pigs of 6 wk of age were pair-fed a control or low lysine (LL) diet. The control diet contained optimal amounts of all essential amino acids, including 1.15% lysine. The LL diet was similar but contained only 0.70% lysine. GLUT4 mRNA expression was upregulated by the LL diet in L. dorsi and rhomboideus muscles, whereas that in cardiac muscle was unaffected. GLUT4 protein abundance was also higher in rhomboideus muscle of animals on the LL diet. We conducted another investigation in order to elucidate effects of the LL diet on post-GLUT4 glucose metabolism. Activity of hexokinase was unaffected by dietary lysine levels while that of citrate synthase was higher both in L. dorsi and rhomboideus muscles of pigs fed on the LL diet. Glucose 6-phosphate content was higher in L. dorsi msucle in the LL group. Glycogen content was higher both in L. dorsi and rhomboideus muscles in the LL group. Further, we determined the effects of dietary lysine levels on accumulation of intramuscular fat (IMF) in L. dorsi muscle of finishing pigs. A low lysine diet (lysine content was 0.40%) meeting approximately 70% of the requirement of lysine was given to finishing pigs for two months. IMF contents in L. dorsi of the pigs given the low lysine diet were twice higher than those of the pigs fed on a control diet (lysine content was 0.65%). Finally, we proved that a well known effect of breadcrumbs feeding to enhance IMF of finishing pigs could be attributed to shortage of amino acids in diets including breadcrumbs.