Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “VALINE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 235 records · Page 13Linked to original sources
PubMed1978

Effects of amino acids on Thiobacillus acidophilus. I. Growth studies with special reference to valine.

The heterotrophic growth of Thiobacillus acidophilus was inhibited by branched-chain amino acids; valine, isoleucine, and leucine. The inhibition by valine and leucine were partially reversed by isoleucine, and the inhibition by isoleucine was partially reversed by valine. Inhibitions by methionine or threonine were partially reversed when both amino acids were present in the growth medium. Inhibition by tyrosine was increased by phenylalanine or tryptophan. Cystine completely inhibited growth. Other amino acids tested produced little or no inhibition. Acetohydroxy acid synthetase (AHAS) activity was demonstrated in crude extracts of T. acidophilus. In crude extracts the optimum pH was 8.5 with a shift to 9.0 in the presence of valine. Valine was the only branched-chain amino acid which inhibited the AHAS activity. The presence of only one peak of AHAS activity upon centrifugation in linear glycerol density gradients demonstrated that the AHAS activity sediments as one component.

Acetolactate Synthase↗
PubMed1979

The effect of L-alpha-amino-n-butyric acid on growth and production of extracellular isoleucine and valine by Eubacterium ruminantium and a related rumen isolate.

Two anaerobic rumen bacteria, Eubacterium ruminantium and a closely related isolate, were studied to determine the effect of the valine antimetabolite alpha-aminobutyric acid on growth and production of extracellular isoleucine and valine in an amino acid free medium. In the absence of alpha-aminobutyrate, these organisms actively excreted valine during growth (90-195 microgram/mL) but only accumulated limited concentrations of isoleucine (3-7 microgram/mL) in the culture broth. Growth of both organisms was reduced in the presence of 0.5-1.5% alpha-aminobutyrate but this inhibition was largely overcome by the use of preadapted inoculum. Metabolism of alpha-aminobutyrate was also increased using preadapted inoculum. During growth in the presence of 0.5-1.5% alpha-aminobutyrate, both organisms accumulated high concentrations of isoleucine (100-225 microgram/mL) while the normal accumulation of valine was unaffected. alpha-Ketobutyrate, a product of alpha-aminobutyrate metabolism, also stimulated isoleucine excretion by these organisms. The results are discussed in relation to the regulation of the biosynthetic pathways of isoleucine and valine in these rumen anaerobes and the potential significance of this amino acid excretion in ruminant nutrition.

Adaptation, Physiological↗
PubMed1977

Serum gonadotropins in rats fed a low-valine diet.

Female rats fed a low-valine diet from the time of weaning have been shown to have delayed puberty compared to growth-matched controls. To explore the mechanism of this delay, serum LH and FSH were measured in rats fed the low-valine diet and in growth-matched control rats at several ages prior to puberty. Hormonal determinations at each time point were made both in the basal state and after LHRH administration or castration. After age 27 days, the mean basal serum FSH was lower in the low-valine group than in the control group. The mean serum levels of LH and FSH after oophorectomy were significantly lower in the low-valine group than in the control group, although the mean serum levels of LH and FSH after LHRH administration to intact animals were similar in both groups. The combination of impaired response to castration with unimpaired pituitary response to LHRH suggests that the low-valine group had a hypothalamic defect which accounts for their delayed sexual maturation when compared to growth-matched animals.

Aging↗
PubMedDate not supplied

Acetohydroxyacid synthase inhibitors: N-phthalyl-L-valine anilide and related compounds.

The potency of L-valine as an inhibitor of Zea mays acetohydroxyacid synthase (AHAS) is increased more than 8000-fold on conversion to its N-phthalyl anilide derivative which is active at 2 microM. The D-valine, alpha-aminobutyric acid, isoleucine and phenylalanine analogs are 11- to 43-fold less potent, and similar N-phthalyl anilide derivatives of other branched-chain amino acids are essentially inactive. Full potency is retained on replacing the phthalimide moiety of the valine anilide with cyclohexane-1,2-dicarboximide or 1-cyclohexene-1,2-dicarboximide groups and partial activity with 4-cyclohexene-1,2-dicarboximide and methyl- or dimethylmaleimide groups. Inhibition of the enzyme and of root growth by the valine derivatives may result from binding at or near the site involved in feedback control of AHAS by L-valine.

Acetolactate Synthase↗
PubMed2006

The dietary valine requirement for prolific lactating sows does not exceed the National Research Council estimate.

Two studies were conducted to determine the effect of increasing the valine:lysine (V:L) ratio in diets of lactating sows above the minimum proposed by the NRC (1998). The first experiment involved 189 PIC, Camborough product sows (parity 1 to 4) that were allotted to 1 of 3 dietary treatments. Diets were formulated to achieve total dietary V:L ratios of 0.90, 1.05, or 1.25:1, respectively, and were corn and soybean meal-based. The second experiment involved 279 PIC, Camborough sows (parity 1 to 5) that were allotted to 1 of 4 treatments. Diets 1 and 3 were formulated using corn and a fixed inclusion of soybean meal (16.7%), with 0.27% L-lysine HCl. The V:L ratios in diets 1 and 3 were 0.73 and 1.25:1, respectively. Diets 2 and 4 were typical corn-soybean meal diets containing 0.05% L-lysine HCl, with a fixed inclusion of soybean meal (22.7%). The V:L ratios in diets 2 and 4 were 0.86 and 1.25:1, respectively. In both experiments, each litter was standardized to a minimum of 10 pigs, which achieved litter growth rates of 2.22 and 2.56 kg/d in Exp. 1 and 2, respectively. In Exp. 1, increasing the dietary V:L ratio beyond 0.90:1 did not improve (P > 0.10) the number of pigs weaned, survival rate, or piglet growth rate, even though sows were nursing more than 10 pigs per litter for 19 d. In Exp. 2, total lysine intake was similar among treatments and ranged from 52.1 to 55.3 g/d. Valine intake increased as the diet valine concentration increased (diet 1 vs. 3 and diet 2 vs. 4, P < 0.001), ranging from 40.0 to 66.1 g/d. Litter gain tended to improve (P = 0.14) when the 0.27% L-lysine HCl control (0.73 V:L) was supplemented with valine to achieve a 1.25:1 V:L ratio. In contrast, no aspect of sow or litter response was improved when the practical control diet containing 0.05% L-lysine HCl (0.86 V:L) was supplemented with valine to achieve a 1.25:1 V:L ratio. Collectively, this research shows that a V:L ratio in excess of 0.86 does not conserve maternal tissue loss or improve piglet growth rate, but a V:L ratio of 0.73 may compromise litter growth rate.

Animal Feed↗
PubMed1992

Inhibition of fibroblast proliferation in L-valine reduced selective media.

A selective cell culture medium, D-valine minimal essential medium (92 mg/l), has been developed to inhibit the proliferation of fibroblasts in cell culture (Gilbert & Migeon 1975). Substitution of D-valine for L-valine prevents fibroblast growth due to the absence of D-amino acid oxidase in these cells. Most cell cultures require foetal bovine serum as an essential component of the culture media, however foetal bovine serum contains L-valine, negating the value of D-valine selective media. To overcome this difficulty, we have produced a modified selective media for cell culture, by the dialysis of foetal bovine serum and confirmed its ability to inhibit fibroblast growth whilst still allowing the proliferation of epithelial cells in culture.

3T3 Cells↗
PubMed2006

Seasonal differences in activities of rabbit liver tRNA and aminoacyl-tRNA synthetases specific for valine and arginine under myocardial ischemia.

UNLABELLED: The objective of this study was to examine the acceptor activities of tRNA for amino acids, valine and arginine, and the activities of the corresponding aminoacyl-tRNA synthetases of normal rabbit liver and 6, 12 and 24 h after experimental myocardial ischemia in different seasons of the year. MATERIAL AND METHODS: Male rabbits (2.5-3.5 kg) were used. Acute myocardial ischemia was induced by occlusion of the left anterior descending coronary artery. tRNA and aminoacyl-tRNA synthetases were isolated from control rabbit liver and 6, 12 and 24 h after experimental myocardial ischemia in autumn (September and October) and winter (December and January). The acceptor activity of tRNA and the activity of valyl- and arginyl-tRNA synthetases were determined using 14C-labeled amino acids, valine and arginine. RESULTS: The results showed that acceptor activity of rabbit liver tRNA for valine and arginine under 6, 12 and 24 h experimental myocardial ischemia in autumn was higher by 24-35% than in winter. Activities of rabbit liver valyl- and arginyl-tRNA synthetases under 6, 12 and 24 h experimental myocardial ischemia in autumn were lower by 15-32% than in winter. No differences in the activity of tRNA and aminoacyl-tRNA synthetases between control groups of both seasons were observed. CONCLUSIONS: The experimental data suggest that acceptor activity of rabbit liver tRNA for valine and arginine and activity of valyl- and arginyl-tRNA synthetases under 6, 12 and 24 h experimental myocardial ischemia are different in autumn and winter. The decrease of acceptor activity of tRNA for valine and arginine after experimental myocardial ischemia correlates with an increase in the activity of valyl- and arginyl-tRNA synthetases both in autumn and winter. It may be part of the compensatory mechanism of the cell to keep synthesis of protein in a normal range under extreme conditions.

Acute Disease↗
PubMed2006

Dietary branched-chain amino acid valine, isoleucine and leucine requirements of fingerling Indian major carp, Cirrhinus mrigala (Hamilton).

Three 8-week growth experiments were conducted to quantify the requirements of the fingerling Cirrhinus mrigala for the dietary branched-chain amino acids valine (experiment 1), isoleucine (experiment 2) and leucine (experiment 3). Six isonitrogenous (400 g/kg) and isoenergetic (17.90 kJ/g) test diets were formulated with a gradation of 2.5 g/kg for each test amino acid, valine (7.5-20 g/kg), isoleucine (5.0-17.5 g/kg) and leucine (7.5-20 g/kg), and fed to randomly stocked fish in circular troughs. In experiment 1, the maximum weight gain (312 %), best feed conversion ratio (FCR; 1.45) and best protein efficiency ratio (PER; 1.72) were obtained in fish fed 15.0 g dietary valine/kg. In experiment 2, the highest weight gain (317 %), best FCR (1.47) and best PER (1.70) were recorded at 12.5 g dietary isoleucine/kg, and in experiment 3, the highest weight gain (308 %), best FCR (1.46) and best PER (1.71) were noted at 15.0 g dietary leucine/kg. A quadratic regression analysis of weight gain, FCR and PER data showed an optimum requirement at 15.9, 15.0 and 14.8 g/kg for valine, 13.2, 12.3 and 12.1 g/kg for isoleucine and 15.6, 15.4 and 15.1 g/kg for leucine in dry diets. Low body moisture and higher protein were noted in fish fed diets containing 15.5, 12.5 and 15.0 g valine, isoleucine and leucine per kg, respectively. Body fat increased with increasing levels of the branched-chain amino acids. On the basis of a regression analysis of growth data, it is recommended that a diet for C. mrigala should contain valine at 15.2, isoleucine at 12.6 and leucine at 15.4 g/kg dry diet, corresponding to 38.0, 31.5 and 38.5 g/kg dietary protein, respectively.

Amino Acids, Branched-Chain↗
PubMed1990

Comparison of deuterated leucine, valine, and lysine in the measurement of human apolipoprotein A-I and B-100 kinetics.

The production rates of apolipoprotein (apo)B-100 in very low density lipoprotein and in low density lipoprotein and apolipoprotein A-I in high density lipoprotein were determined using a primed-constant infusion of [5,5,5,-2H3]leucine, [4,4,4,-2H3]valine, and [6,6-2H2,1,2-13C2]lysine. The three stable isotope-labeled amino acids were administered simultaneously to determine whether absolute production rates calculated using a stochastic model were independent of the tracer species utilized. Three normolipidemic adult males were studied in the constantly fed state over a 15-h period. The absolute production rates of very low density lipoprotein apoB-100 were 11.4 +/- 5.8 (leucine), 11.2 +/- 6.8 (valine), and 11.1 +/- 5.4 (lysine) mg per kg per day (mean +/- SDM). The absolute production rates for low density lipoprotein apoB-100 were 8.0 +/- 4.7 (leucine), 7.5 +/- 3.8 (valine), and 7.5 +/- 4.2 (lysine) mg per kg per day. The absolute production rates for high density lipoprotein apoA-I were 9.7 +/- 0.2 (leucine), 9.4 +/- 1.7 (valine, and 9.1 +/- 1.3 (lysine) mg per kg per day. There were no statistically significant differences in absolute synthetic rates of the three apolipoproteins when the plateau isotopic enrichment values of very low density lipoprotein apoB-100 were used to define the isotopic enrichment of the intracellular precursor pool. Our data indicate that deuterated leucine, valine, or lysine provided similar results when used for the determination of apoA-I and apoB-100 absolute production rates within plasma lipoproteins as part of a primed-constant infusion protocol.

Adult↗
PubMed1982

Production of L-[1-11C]valine by HPLC resolution.

Based on a recently developed analytical technique, preparative high-performance liquid chromatographic (HPLC) resolution of DL-[1-11C]valine has been achieved. A conventional reverse-phase HPLC column and a chiral mobile phase (aqueous solution of L-proline, cupric acetate, and sodium acetate) were used. The copper can be removed from the L-valine fraction by precipitation as the sulfide, and final purification by cation-exchange chromatography yields L-[1-11C]valine in a form that is acceptable for clinical positron tomographic studies. This purification method does not remove the L-proline introduced in the resolution process, but added L-proline did not affect the tissue distribution of L-[1-14C]valine in rats. We have produced up to 60 mCi of L-[1-11C]valine in an overall synthesis and resolution time of 50 min. This procedure should be adaptable to the rapid resolution of other C-11-labeled amino acid racemates.

Carbon Radioisotopes↗
PubMed1989

Purification and catalytic properties of L-valine dehydrogenase from Streptomyces cinnamonensis.

NAD+-dependent L-valine dehydrogenase was purified 180-fold from Streptomyces cinnamonensis, and to homogeneity, as judged by gel electrophoresis. The enzyme has an Mr of 88,000, and appears to be composed of subunits of Mr 41,200. The enzyme catalyses the oxidative deamination of L-valine, L-leucine, L-2-aminobutyric acid, L-norvaline and L-isoleucine, as well as the reductive amination of their 2-oxo analogues. The enzyme requires NAD+ as the only cofactor, which cannot be replaced by NADP+. The enzyme activity is significantly decreased by thiol-reactive reagents, although purine and pyrimidine bases, and nucleotides, do not affect activity. Initial-velocity and product-inhibition studies show that the reductive amination proceeds through a sequential ordered ternary-binary mechanism; NADH binds to the enzyme first, followed by 2-oxoisovalerate and NH3, and valine is released first, followed by NAD+. The Michaelis constants are as follows; L-valine, 1.3 mM; NAD+, 0.18 mM; NADH, 74 microM; 2-oxoisovalerate, 0.81 mM; and NH3, 55 mM. The pro-S hydrogen at C-4' of NADH is transferred to the substrate; the enzyme is B-stereospecific. It is proposed that the enzyme catalyses the first step of valine catabolism in this organism.

Amination↗
PubMed1981

Nucleotide sequence of a spinach chloroplast valine tRNA.

The nucleotide sequence of a spinach chloroplast valine tRNA (sp. chl. tRNA Val) has been determined. This tRNA shows essentially equal homology to prokaryotic valine tRNAs (58-65% homology) and to the mitochondrial valine tRNAs of lower eukaryotes (yeast and N. crassa, 61-62% homology). Sp. chl. tRNA Val shows distinctly lower homology to mouse mitochondrial valine tRNA (53% homology) and to eukaryotic cytoplasmic valine tRNAs (47-53% homology). Sp. chl. tRNA Val, like all other chloroplast tRNAs sequenced, contains a methylated GG sequence in the dihydrouridine loop and lacks unusual structural features which have been found in several mitochondrial tRNAs.

Animals↗
PubMed1985

Reversal of chlorsulfuron-induced inhibition of mitotic entry by isoleucine and valine.

Pea (Pisum sativum L. cv Alaska) root tips were excised and cultured aseptically in White's medium. Cultures were treated immediately or after a 24 hour equilibration time with 28 nanomolar chlorsulfuron plus isoleucine and valine (each 0.1 millimolar), isoleucine and valine, or untreated. The percentage of mitotic figures in untreated control roots sampled immediately after excision showed a transitory drop and recovery within 24 hours (an excision effect). In chlorsulfuron-treated roots, the percentage of mitotic figures did not recover. In roots treated with chlorsulfuron plus isoleucine and valine, a complete recovery did occur. If roots were treated with chlorsulfuron 24 hours after excision, the percentage of mitotic figures was reduced to near 0 by 8 hours. In roots treated with chlorsulfuron plus isoleucine and valine, no reduction in mitotic figures occurred. The complete reversal of chlorsulfuron-inhibited mitotic entry by isoleucine and valine implicates these amino acids, in some manner, with the control of cell cycles progression.

Journal Article↗
PubMed1998

In vivo determination of very-low-density lipoprotein-apolipoprotein B100 secretion rates in humans with a low dose of l-[1-13C]valine and isotope ratio mass spectrometry.

The aim of the present study was to determine the rate of very-low-density lipoprotein (VLDL)-apolipoprotein (apo) B100 secretion in humans with a minimized amount of l-[1-13C]valine infusion in combination with the use of gas chromatography/combustion/isotope ratio mass spectrometry (GC/C/IRMS) analysis. To compare this method with the conventional gas chromatography/mass spectrometry (GC/MS) technique, two different dosages of l-[1-13C]valine and both analytical techniques were compared in a single study. A priming dose of l-[1-13C]valine (2 micromol/kg) followed by a constant infusion (2 micromol/kg/h) was given for 3 h, directly followed by a second priming dose (15 micromol/kg) and a constant infusion (15 micromol/kg/h) for 4 h. The fractional secretion rate obtained by GC/C/IRMS measurements from the first 3 h of infusion (mean +/- SD: 0.22 +/- 0.09 pools/h) was similar to that obtained by GC/MS during the last 4 h of infusion (0. 23 +/- 0.07 pools/h; P = 0.56). In conclusion, superior analytical accuracy and sensitivity of GC/C/IRMS enable measurements of VLDL-apo B100 secretion with much lower doses of l-[1-13C]valine and allow for reduction of experimental costs.

Apolipoprotein B-100↗
PubMed1998

Isolated isobutyryl-CoA dehydrogenase deficiency: an unrecognized defect in human valine metabolism.

A 2-year-old female was well until 12 months of age when she was found to be anemic and had dilated cardiomyopathy. Total plasma carnitine was 6 microM and acylcarnitine analysis while receiving carnitine supplement revealed an increase in the four-carbon species. Urine organic acids were normal. In vitro analysis of the mitochondrial pathways for beta oxidation, and leucine, valine, and isoleucine metabolism was performed in fibroblasts using stable isotope-labeled precursors to these pathways followed by acylcarnitine analysis by tandem mass spectrometry. 16-2H3-palmitate was metabolized normally down to the level of butyryl-CoA thus excluding SCAD deficiency. 13C6-leucine and 13C6-isoleucine were also metabolized normally. 13C5-valine incubation revealed a significant increase in 13C4-isobutyrylcarnitine without any incorporation into propionylcarnitine as is observed normally. These same precursors were also evaluated in fibroblasts with proven ETF-QO deficiency in which acyl-CoA dehydrogenase deficiencies in each of these pathways was clearly identified. These results indicate that in the human, there is an isobutyryl-CoA dehydrogenase which exists as a separate enzyme serving only the valine pathway in addition to the 2-methyl branched-chain dehydrogenase which serves both the valine and the isoleucine pathways in both rat and human.

Cardiomyopathies↗
PubMed1996

A single amino acid change in acetolactate synthase confers resistance to valine in tobacco.

The metabolic control of branches chain amino acid (BCAA) biosynthesis involves allosteric regulation of acetolactate synthase (ALS) by the end-products of the pathway, valine, leucine and isoleucine. We describe here the molecular basis of valine resistance. We cloned and sequenced an ALS gene from the tobacco mutant Valr-1 and found a single basepair substitution relative to the wild-type allele. This mutation causes a serine to leucine change in the amino acid sequence of ALS at position 214. We then mutagenized the wild-type allele of the ALS gene of Arabidopsis and found that it confers valine resistance when introduced into tobacco plants. Taken together, these results suggest that the serine to leucine change at position 214 of ALS is responsible for valine resistance in tobacco.

Acetolactate Synthase↗
PubMed1992

Evidence that the large neutral amino acid L-valine decreases electrically-evoked release of 5-HT in rat hippocampus in vivo.

L-Valine competes with tryptophan for transport into the brain and has previously been shown to decrease brain 5-HT synthesis. In the present study, the effect of L-valine on electrically evoked hippocampal 5-HT release was determined in the anaesthetized rat using microdialysis. In control animals two electrical stimulations of the dorsal raphe nucleus 120 min apart (S1 and S2, respectively) released similar amounts of 5-HT. In contrast, in animals which received L-valine (200 mg/kg) between stimulations, S2 released a significantly smaller amount of 5-HT than did S1, although basal 5-HT release was unchanged. The data demonstrate that L-valine decreases the electrically-evoked release of 5-HT in hippocampus in vivo.

Animals↗
PubMed2002

Production of teicoplanin by valine analogue-resistant mutant strains of Actinoplanes teichomyceticus.

Teicoplanin is a glycopeptide antibiotic produced by Actinoplanes teichomyceticus. A strain improvement to increase the productivity of the major component, teicoplanin A2-2, was carried out. As the fatty moiety of teicoplanin A2-2 is derived from L-valine, L-valine analogue (valine hydroxamate)-resistant mutants were derived. One of the mutants, 98-1-227, overproduced valine and produced a higher titer of total teicoplanin with higher A2-2 content. In a pilot fermentor (7 m3), the total productivity of teicoplanin was 1,800 units/ml and the A2-2 content was 58%.

Actinomycetales↗