Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “METHIONINE”

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 73 records · Page 4Linked to original sources
PubMed1991

Homocysteine export from cells cultured in the presence of physiological or superfluous levels of methionine: methionine loading of non-transformed, transformed, proliferating, and quiescent cells in culture.

Determination of the transient increase in plasma homocysteine following administration of excess methionine is an established procedure for the diagnosis of defects in homocysteine metabolism in patients. This so-called methionine loading test has been used for 25 years, but the knowledge of the response of various cell types to excess methionine is limited. In the present paper we investigated homocysteine export from various cell types cultured in the presence of increasing concentrations (15-1,000 microM) of methionine. For comparison of homocysteine export, the export rates per million cells were plotted versus cell density for proliferating cells, and versus time for quiescent cells. The homocysteine export from growing cells was greatest during early to mid-exponential growth phase, and then decreased as a function of cell density. The export rate was higher from phytohemagglutinin-stimulated than non-stimulated lymphocytes, and higher from proliferating than from quiescent fibroblasts. The hepatocytes showed highest export rate among the cell types investigated. The enhancement of homocysteine export by excess methionine ranged from no stimulation to marked enhancement, depending on cell type investigated, and three different response patterns could be distinguished: 1) quiescent fibroblasts and growing murine lymphoma cell showed no significant increase in homocysteine export following methionine loading; export from human lymphocytes was only slightly enhanced in the presence of excess methionine; 2) the homocysteine export from proliferating hepatoma cells and benign and transformed fibroblasts was stimulated three to eightfold by increasing the methionine concentration in the medium from 15 to 1,000 microM; and 3) the response to methionine loading was particularly increased (about 15-fold) in non-transformed primary hepatocytes in stationary culture. The results outline a potentially useful procedure for the comparison of homocysteine export during cell growth in the presence of various concentrations of methionine. The results are discussed in relation to the special feature of homocysteine metabolism in various cell types and tissues including liver, and to the possible source of plasma homocysteine following methionine loading in vivo.

Animals↗
PubMed2002

Remethylation and transsulfuration of methionine in cirrhosis: studies with L-[H3-methyl-1-C]methionine.

Disturbances of the methionine cycle may result in liver injury. Patients with alcohol-induced liver disease often exhibit hypermethioninemia and a delayed clearance (CL) of methionine, but the extent to which transsulfuration and remethylation pathways of the cyclic methionine metabolism are affected is unknown. Methionine turnover was determined in 7 healthy volunteers and 6 patients with alcohol-induced cirrhosis after oral administration of 2 mg/kg [(2)H(3)-methyl-1-(13)C]methionine, which permitted us to follow transsulfuration by its decarboxylation to (13)CO(2) and remethylation by replacement of the labeled methyl group by an unlabeled one. Basal plasma concentrations of endogenous methionine (50 +/- 5 vs. 25 +/- 2 micromol/L, mean +/- SEM, P <.001) were significantly higher in patients with cirrhosis and its CL was significantly decreased (774 +/- 103 vs. 2,050 +/- 141 mL/min, P <.001). Methionine turnover amounted to 42 +/- 4 vs. 27 +/- 3 micromol/kg/h (P <.05) in controls and patients with cirrhosis, respectively. The fraction of administered methionine undergoing remethylation was lower in patients with cirrhosis (7.6 +/- 1.5 vs. 14.1 +/- 1.1%, P <.005). However, because of the larger pool of circulating methionine, the total flux of methionine through the remethylation pathway was similar in both groups. A significantly lower fraction of the administered dose appeared in the form of (13)CO(2) in breath in patients with cirrhosis (2.2 +/- 0.4 vs. 11.0 +/- 0.8%, P <.001). In conclusion, the data indicate that the liver with cirrhosis compensates for a decreased activity of remethylating enzymes by operating at higher concentrations of methionine. In contrast, transsulfuration is impaired in patients with alcohol-induced cirrhosis such that an assessment of transsulfuration by a simple breath test may provide a clinically useful estimate of hepatic function.

Adult↗
PubMed1995

[Methodical investigations on the metabolism oriented determination of methionine requirement of broiler chickens. 3. Degradation of 14C-(CH3)- and 35S-methionine after feeding of synthetic diets].

In a chicken experiment was investigated, whether the kind of applied isotope and labelling site influence the results of the metabolism oriented estimation of the methionine requirement. Furthermore it was studied, if this method can give additional informations to weight gain and N-retention data concerning methionine requirement. 48 male broiler chickens received synthetic diets with a complete amino acid mixture from day 7 posthatching. The methionine content of the 8 experimental diets varied from 2.25 to 7.5 g methionine/kg DM (1.17 to 3.87 g/16 g N). The low weight gain (13 to 22 g/d) and N-retention (0.55 to 0.87 g/d; from day 13 to 17 posthatching) was due to the inferior intake of the synthetic diets. Methionine supplementation increased weight gain and N-retention only up to 3 g methionine/kg DM. The metabolic methionine requirement was measured after i.v. injection of 14C-(CH3)- and 35S-methionine by 14CO2-excretion with breath and 35S-excretion with excrements. Both parameters gave similar results and showed an increased methionine degradation at methionine contents exceeding 4.5 g methionine/kg DM. Because there was no increase in methionine degradation up to 4.5 g/kg DM, an increased reutilization of methionine within the range between 3 and 4.5 g methionine/kg DM was supposed, which may act as a spare-mechanism. For practical feeding applications, also in case of low feed intake, a minimal methionine content of 4.5 g/kg DM is recommended.

Amino Acids↗
PubMed1997

Effect of cystine intake on methionine kinetics and oxidation determined with oral tracers of methionine and cysteine in healthy adults.

There is evidence based on nitrogen balance that dietary cystine spares, from approximately 16% to 89%, the total methionine requirement. In a previous study we did not detect, by tracer techniques, a sparing effect of cystine when the diet provided methionine at a limiting intake (requirement level: 13 mg.kg-1.d-1). One reason could be that we used an intravenous infusion of the tracer, which may not, therefore, have labeled the carbon dioxide derived from the splanchnic oxidation of dietary methionine. The aim of this study was to compare methionine metabolism and oxidation in eight healthy adults given for 6 d each of three different diets: 13 mg (87.0 mumol) methionine.kg-1.d-1 and no cystine (diet A); 5 mg (33.5 mumol) methionine.kg-1.d-1 and no cystine (diet B); and 5 mg (33.5 mumol) methionine.kg-1.d-1 and 6.5 mg (52.4 mumol) cystine.kg-1.d-1 (diet C). On day 7, tracers ([1-13C, methyl-2H3]methionine and [2H2]cysteine) were administered orally at 30-min intervals for 8 h. Blood and breath samples were obtained for analysis during 3-h fasting and consecutive 5-h feeding periods. During fasting, methionine oxidation and methionine methyl (Qm) and carboxyl (Qc) fluxes and plasma concentrations were not affected by the amount of sulfur amino acids in the three diets. In the fed state methionine oxidation was significantly lower during diets B (3.0 +/- 0.5 mumol.kg-1.h-1) and C (2.8 +/- 0.6 mumol.kg-1.h-1) than during diet A (4.1 +/- 0.9 mumol.kg-1.h-1); there were no significant differences between diets B and C. Qm and Qc decreased with decreased methionine intake but no effect was observed by adding cystine. Cysteine flux (Qcys) was not affected by diet composition but it was lower during feeding than during fasting. In conclusion, replacing approximately 60% of the total requirement for methionine with cystine over a short diet period did not result in a detectable sparing of methionine oxidation.

Adult↗
PubMed1987

Metabolism of methionine and methionine hydroxy analogue by porcine kidney fibroblasts.

Porcine kidney fibroblasts in culture are able to utilize the 2-hydroxy analog of methionine (MHA) as the sole methionine source, but higher concentrations of MHA than methionine are required. The optimal concentration for growth with L-methionine ranges from 0.02 to 1.0 mM, whereas that for DL-MHA is 7.5 mM. At concentrations above 1.0 mM, L-methionine exhibits a toxic effect. Supplementing 1.0 mM L-methionine with DL-MHA allows greater growth than that provided by an equimolar concentration of L-methionine alone, and no toxic effect is seen at methionine source (DL-MHA) concentrations up to 7.5 mM. Early in the growth phase of cells where DL-MHA is the sole source of methionine, a 48-h lag period is observed over that seen in cells grown in the presence of 1.0 mM L-methionine. After the lag period, the MHA-supplemented cells double at the same rate as the methionine-supplemented cells. Studies with the purified isomers of D- and L-MHA indicate that only the D-isomer is utilized by these fibroblasts.

Animals↗
PubMed1992

Methionine intake in rainbow trout (Oncorhynchus mykiss), relationship to cataract formation and the metabolism of methionine.

Young rainbow trout were given diets containing graded levels of methionine for 16 wk. Analysis of the weight gain and food efficiency data showed the methionine requirement to be not more than 0.76% of the diet (1.9% of dietary protein). Activities of regulatory enzymes of the transulfuration pathway, methionine adenosyltransferase and cystathionine synthase in trout liver were not altered by changes in methionine intake. Concentrations of free serine in liver and plasma of the trout were high at low levels of methionine intake but fell as dietary methionine increased. This implied decreased flux through cystathionine synthase at low methionine intakes. Large increases in liver and plasma taurine occurred at high methionine intakes, implying enhanced transulfuration activity. Liver ornithine decarboxylase activity was reduced at the lowest level of dietary methionine used but the activity of S-adenosylmethionine decarboxylase was unchanged. Eye lenses of the trout given these diets were examined by a scanning lens monitor. Analysis of focal length variability with this equipment demonstrated that, if abnormality of the lens is to be avoided, a higher concentration of dietary methionine (0.96% or 0.6% methionine + 0.36% cystine) is needed than that required to maximize growth.

Amino Acids↗
PubMed1973

Methionine limitation in Escherichia coli K-12 by growth on the sulfoxides of D-methionine.

The synthesis and resolution of the diastereoisomers of d-methionine sulfoxide in high yield is described. Growth of two methionine auxotrophs (strains HfrC and AB1932) on the d-methionine sulfoxides is slower than on l-methionine, and the resultant cells are markedly derepressed for three enzymes of the methionine regulon (cystathionine synthetase, cystathionase, and S-adenosyl-l-methionine synthetase). Strain HfrC grows more rapidly on the sulfoxides and shows less derepression than strain AB1932. Although growth on d-methionine-d-sulfoxide is much slower than on d-methionine-l-sulfoxide (two- to threefold increase in division times), cells grown on d-methionine-l-sulfoxide generally have higher enzyme activities. The sulfoxides of d-methionine appear to provide a useful supplement to obtain methionine-limited growth in Escherichia coli.

Adenosine Triphosphate↗
PubMed1993

Methionine synthase inactivation by nitrous oxide during methionine loading of normal human fibroblasts. Homocysteine remethylation as determinant of enzyme inactivation and homocysteine export.

Nitrous oxide inactivates the enzyme methionine synthase by oxidation of enzyme bound cobalamin, which is formed from the cofactor methylcobalamin during the catalytic cycle. The resulting inhibition of homocysteine remethylation increases the homocysteine efflux and thereby the level of extracellular homocysteine, both in patients and cultured cells. In the present work we measured the kinetics of enzyme inactivation and homocysteine export rate in two human fibroblast cell lines exposed to nitrous oxide and cultured in the presence of low to supraphysiological concentrations (15-100 microM) of methionine. Both the rate and extent of methionine synthase inactivation were reduced by increasing methionine concentration in the culture medium. In cells not exposed to nitrous oxide, methionine increased the homocysteine export rate in a dose-dependent manner. Nitrous oxide increased the export at low methionine concentrations, so that for treated cells the export was high and essentially independent of the extracellular methionine level. Neither methionine nor nitrous oxide significantly affected the amount of S-adenosylmethionine or folate in these cells. These data agree with methionine synthase as a low Km and methionine conserving enzyme, highlight the importance of methionine synthase activity as a determinant of homocysteine export and point to the possibility of protecting the enzyme by reducing catalytic turnover through product inhibition.

5-Methyltetrahydrofolate-Homocysteine S-Methyltran↗
PubMed1999

Methionine S-oxidation in human and rabbit liver microsomes: evidence for a high-affinity methionine S-oxidase activity that is distinct from flavin-containing monooxygenase 3.

Methionine has previously been shown to be S-oxidized by flavin-containing monooxygenase (FMO) forms 1, 2, and 3. The most efficient catalyst was FMO3, which has a Km value for methionine S-oxidation of approximately 4 mM, and exhibits high selectivity for formation of the d-diastereoisomer of methionine sulfoxide. The current studies provide evidence for an additional methionine S-oxidase activity in liver microsomes. Human and rabbit liver microsomes exhibited a biphasic response to methionine at concentrations ranging from 0.05 to 10 mM, as indicated by both Eadie-Hofstee plots and nonlinear regression. The low-affinity component of the biphasic response had Km values of approximately 3 and 5 mM for humans and rabbits, respectively, as well as high diastereoselectivity for methionine sulfoxide formation. The low-affinity activity in rabbit liver microsomes was inhibited by methimazole, S-allyl-l-cysteine, and by mild heat treatment, suggesting the activity is FMO3. The high-affinity component of the biphasic response had Km values of approximately 0.07 and 0.04 mM for humans and rabbits, respectively, as well as lower diastereoselectivity for methionine sulfoxide formation. Further characterization of the high-affinity activity in rabbit liver microsomes indicated lack of involvement of cytochrome P450s or reactive oxygen species. The high-affinity activity was inhibited 25% by potassium cyanide and greater than 50% by methimazole and S-allyl-l-cysteine. Mild heat treatment produced 85% inhibition of the low-affinity activity, but only 30% inhibition of the high-affinity activity. Both high- and low-affinity activities were decreased by 85% in flavin-depleted microsomes. Because these results suggested the additional S-oxidase activity has characteristics of an FMO, recombinant human FMO4 was evaluated as a potential catalyst of this activity. Recombinant FMO4 catalyzed S-oxidation of both methionine and S-allyl-l-cysteine, with similar diastereoselectivity to the high-affinity microsomal S-oxidase; however, the Km values for both reactions appeared to be greater than 10 mM. In summary, these studies provide evidence for two microsomal methionine S-oxidase activities. FMO3 is the predominant catalyst at millimolar concentrations of methionine. However, at micromolar methionine concentrations, there is an additional S-oxidase activity that is distinct from FMO3.

Adult↗
PubMed1970

Identification of L-methionine-S-sulfoximine as the convulsant isomer of methionine sulfoximine.

The convulsant agent methionine sulfoximine inhibits brain glutamine synthetase irreversibly and the inhibitor becomes bound to the active site of the enzyme as methionine sulfoximine phosphate. Only one of the four isomers of methionine sulfoximine, L-methionine-S-sulfoximine, inhibits glutamine synthetase. In the present work, D-methionine-SR-sulfoximine, and highly purified preparations of L-methionine-S-sulfoximine and L-methionine-R-sulfoximine were tested in mice for convulsant activity; only L-methionine-S-sulfoximine produced convulsions. The finding that only one of the four optical isomers of methionine sulfoximine induces convulsions, and that only this same isomer inhibits glutamine synthetase, lends support to the conclusion that these two effects of methionine sulfoximine are closely connected.

Animals↗
PubMed2003

L-methionine availability regulates expression of the methionine adenosyltransferase 2A gene in human hepatocarcinoma cells: role of S-adenosylmethionine.

In mammals, methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (AdoMet) synthesis, is encoded by two genes, MAT1A and MAT2A. In liver, MAT1A expression is associated with high AdoMet levels and a differentiated phenotype, whereas MAT2A expression is associated with lower AdoMet levels and a dedifferentiated phenotype. In the current study, we examined regulation of MAT2A gene expression by l-methionine availability using HepG2 cells. In l-methionine-deficient cells, MAT2A gene expression is rapidly induced, and methionine adenosyltransferase activity is increased. Restoration of l-methionine rapidly down-regulates MAT2A mRNA levels; for this effect, l-methionine needs to be converted into AdoMet. This novel action of AdoMet is not mediated through a methyl transfer reaction. MAT2A gene expression was also regulated by 5'-methylthioadenosine, but this was dependent on 5'-methylthioadenosine conversion to methionine through the salvage pathway. The transcription rate of the MAT2A gene remained unchanged during l-methionine starvation; however, its mRNA half-life was significantly increased (from 100 min to more than 3 h). The effect of l-methionine withdrawal on MAT2A mRNA stabilization requires both gene transcription and protein synthesis. We conclude that MAT2A gene expression is modulated as an adaptive response of the cell to l-methionine availability through its conversion to AdoMet.

Carcinoma, Hepatocellular↗
PubMed2003

N-terminal methionine removal and methionine metabolism in Saccharomyces cerevisiae.

Methionine aminopeptidase (MetAP) catalyzes removal of the initiator methionine from nascent polypeptides. In eukaryotes, there are two forms of MetAP, type 1 and type 2, whose combined activities are essential, but whose relative intracellular roles are unclear. Methionine metabolism is an important aspect of cellular physiology, involved in oxidative stress, methylation, and cell cycle. Due to the potential of MetAP activity to provide a methionine salvage pathway, we evaluated the relationship between methionine metabolism and MetAP activity in Saccharomyces cerevisiae. We provide the first demonstration that yeast MetAP1 plays a significant role in methionine metabolism, namely, preventing premature activation of MET genes through MetAP function in methionine salvage. Interestingly, in cells lacking MetAP1, excess methionine dramatically inhibits cell growth. Growth inhibition is independent of the ability of methionine to repress MET genes and does not result from inhibition of synthesis of another metabolite, rather it results from product inhibition of MetAP2. Inhibition by methionine is selective for MetAP2 over MetAP1. These results provide an explanation for the previously observed dominance of MetAP1 in terms of N-terminal processing and cell growth in yeast. Additionally, differential regulation of the two isoforms may be indicative of different intracellular roles for the two enzymes.

Aminopeptidases↗
PubMed1985

Comparative metabolism of L-methionine, DL-methionine and DL-2-hydroxy 4-methylthiobutanoic acid by broiler chicks.

1. Metabolism, in broiler chicks, of DL-2-hydroxy 4-methylthiobutanoic acid (DL-HMB), DL-methionine and L-methionine was compared in vivo using 14C-labelled tracers. 2. The distribution of L-[1-14C]methionine and DL-[1-14C]HMB in the major body tissues was examined for a period of 120 min after administration. 3. The relative oxidation (14CO2 exhaled), excretion and incorporation into tissue protein of L-[1-14C]methionine, DL-[1-14C]methionine and DL-[1-14C]HMB were measured in fed birds. 4. Tissue distribution of L-[1-14C]methionine and DL-[1-14C]HMB differed during 60-90 min following administration. 5. The production of 14CO2 from each of the tracers was similar but excretion of 14C-labelled material was very different with the greatest excretion from DL-[1-14C]HMB and the least from L-[1-14C]methionine. 6. The incorporation of 14C into tissue proteins varied with the tracer given and the tissue examined. Liver and kidney had equivalent incorporation from each of the tracers while other tissues examined showed lower incorporation from DL-[1-14C]methionine and DL-[1-14C]HMB. 7. The results show that DL-HMB, D-methionine and L-methionine are metabolized differently in vivo and that they are excreted in differing proportions. There is also a difference in the ability of each to act as a precursor for protein synthesis in tissues other than liver.

Animals↗
PubMed1996

Peptide-bound methionine can be a source of methionine for the synthesis of secreted proteins by mammary tissue explants from lactating mice.

Mammary tissue explants from d 10-11 of lactating CD-1 mice were used to study the ability of methionine-containing di- to octapeptides to substitute for free methionine for the synthesis of secreted proteins. Explants were incubated in a medium containing 3H-leucine and either L-methionine or one of 23 methionine-containing peptides. The ability of methionine substrates to promote incorporation of 3H-leucine into secreted proteins was quantified. Mammary tissue explants were able to utilize methionine from all peptides tested. All of the peptides were at least as effective as free methionine in promoting 3H-leucine incorporation into secreted proteins. Most di- and tripeptides promoted 15-76% greater (P < 0.05) 3H-leucine incorporation than did free methionine. There was a negative correlation (r = -0.89, P < 0.01) between the rate of 3 H-leucine incorporation promoted by peptides and the number of amino acid residues in the peptides. The incorporation of 3H-leucine promoted by some dipeptides was reduced (P < 0.05) in the presence of a 200-fold higher concentration of glycylsarcosine or carnosine. The results indicate that peptide-bound methionine can serve as a source of methionine for the synthesis of secreted proteins by lactating mammary tissue. Mediated transport of some peptides is probably involved in peptide utilization.

Amino Acid Sequence↗
PubMed2005

Soluble methionine enhances accumulation of a 15 kDa zein, a methionine-rich storage protein, in transgenic alfalfa but not in transgenic tobacco plants.

With the general aim of elevating the content of the essential amino acid methionine in vegetative tissues of plants, alfalfa (Medicago sativa L.) and tobacco plants, as well as BY2 tobacco suspension cells, were transformed with a beta-zein::3HA gene under the 35S promoter of cauliflower mosaic virus encoding a rumen-stable methionine-rich storage protein of 15 kDa zein. To examine whether soluble methionine content limited the accumulation of the 15 kDa zein::3HA, methionine was first added to the growth medium of the different transgenic plants and the level of the alien protein was determined. Results demonstrated that the added methionine enhanced the accumulation of the 15 kDa zein::3HA in transgenic alfalfa and tobacco BY2 cells, but not in whole transgenic tobacco plants. Next, the endogenous levels of methionine were elevated in the transgenic tobacco and alfalfa plants by crossing them with plants expressing the Arabidopsis cystathionine gamma-synthase (AtCGS) having significantly higher levels of soluble methionine in their leaves. Compared with plants expressing only the 15 kDa zein::3HA, transgenic alfalfa co-expressing both alien genes showed significantly enhanced levels of this protein concurrently with a reduction in the soluble methionine content, thus implying that soluble methionine was incorporated into the 15 kDa zein::3HA. Similar phenomena also occurred in tobacco, but were considerably less pronounced. The results demonstrate that the accumulation of the 15 kDa zein::3HA is regulated in a species-specific manner and that soluble methionine plays a major role in the accumulation of the 15 kDa zein in some plant species but less so in others.

Base Sequence↗
PubMed1976

An evaluation of the L-methionine activity of the hydroxy analogue of methionine.

Three product forms of methionine hydroxy analogue were prepared for biological evaluation of their L-methionine activity for broiler strain chickens (Vantress x Arbor Acres). Two samples of the acid of the analogue HA-50, LMA-70 and one sample of a commercial grade (90%) MHA were standarized by gas liquid chromatography to contain a known amount of L-methionine activity as the free analogue acid. Each product form was tested in a separate experiment. The experimental chickens were fed a practical corn-soybean meal basal diet for the first seven days of the test. A semi-purified diet composed primarily of cerelose, isolated soybean protein and soybean meal was used for the remainder of the experimental period. HA-50 and the commercial form of the hydroxy analogue were formulated to contain 50% L-methionine activity. Hence, they were added to the diets at 0.1 and 0.2% and compared to the L-methionine standard which was added to levels of 0.05, 0.1 and 0.15%. LMA-70 was formulated to contain 70% L-methionine activity and was added to the experimental diets at 0.07 and 0.14% and compared to the L-methionine standard at the same levels used in the other experiments. Statistical analysis of four-week data revealed no difference between the biological response of L-methionine and the three forms of the analogue when tested at comparable L-methionine activity levels. The biological of the analogue products was in good agreement with the L-methionine activity determined by gas liquid chromatography.

Animal Feed↗
PubMed1988

Comparison of L-[1-11C]methionine and L-methyl-[11C]methionine for measuring in vivo protein synthesis rates with PET.

To evaluate the feasibility of using either L-[1-11C]-methionine or L-[methyl-11C]methionine for measuring protein synthesis rates by positron emission tomography (PET) in normal and neoplastic tissues, distribution and metabolic studies with 14C- and 11C-labeled methionines were carried out in rats bearing Walker 256 carcinosarcoma. The tissue distributions of the two 14C-labeled methionines were similar except for liver tissue. Similar distribution patterns were observed in vivo by PET using 11C-labeled methionines. The highest 14C incorporation rate into the protein-bound fraction was found in the liver followed by tumor, brain, and pancreas. The incorporation rates in liver and pancreas were different for the two methionines. By chloroform-methanol fractionation of these four tissues, in liver significantly different amounts of 14C were observed in macromolecules. Also in brain tissue slight differences were found. By HPLC analyses of the protein-free fractions of plasma, tumor, and brain tissue at 60 min after injection, for both methionines several 14C-labeled metabolites in different amounts, were detected. About half of the 14C-labeled material in the protein-free fraction was found to be methionine. In these three tissues the amount of nonprotein metabolites and [14C]bicarbonate amount ranged from 10% to 17% and 12% to 15% for L-[1-14C]methionine and L-[methyl-14C]methionine, respectively. From these results it can be concluded that the minor metabolic pathways have to be investigated in order to quantitatively model the protein synthesis by PET.

Animals↗
PubMed1996

Toxicity of seleno-L-methionine, seleno-DL-methionine, high selenium wheat, and selenized yeast to mallard ducklings.

The toxicity of four chemical forms of selenium (seleno-L-methionine, seleno-DL-methionine, selenized yeast, and high selenium wheat) was compared in day-old mallard ducklings (Anas platyrhynchos). In the first experiment, in which the basal diet was 75% wheat, survival after 2 weeks was lower for ducklings fed 30 micrograms/g selenium as seleno-L-methionine (36%) than for ducklings fed 30 micrograms/g selenium as seleno-DL-methionine (100%) or 30 micrograms/g selenium from high selenium yeast (88%). The concentration of selenium at 2 weeks in the livers of survivors was similar for ducklings fed 15 micrograms/g selenium as seleno-DL-methionine (12 micrograms/g, wet weight), seleno-L-methionine (11 micrograms/g), and high selenium wheat (11 micrograms/g), but was lower when the selenium came from selenized yeast (6.2 micrograms/g). When fed 30 micrograms/g selenium from the various sources, the selenium concentrations in liver were 20 micrograms/g for seleno-DL-methionine, 19 micrograms/g for seleno-L-methionine, and 9.9 micrograms/g for selenized yeast. In a second experiment, in which the basal diet was a commercial duck feed, survival after 2 weeks was 100% in ducklings fed 30 micrograms/g selenium as seleno-DL-methionine, seleno-L-methionine, or selenized yeast. Selenium concentrations in liver were similar for ducklings fed the 30-micrograms/g selenium diets as the DL or L forms of selenomethionine (27 and 25 micrograms/g), but lower for ducklings fed selenized yeast (13 micrograms/g).(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗