Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “LIPOIC ACID”

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 1,171 records · Page 65Linked to original sources
PubMed1964

CULTIVATION OF LEPTOSPIRAE. I. NUTRITION OF LEPTOSPIRA CANICOLA.

Stalheim, O. H. V. (University of Wisconsin, Madison), and J. B. Wilson. Cultivation of leptospirae. I. Nutrition of Leptospira canicola. J. Bacteriol. 88:48-54. 1964.-The nutrition of Leptospira canicola was investigated by use of synthetic media of suitable ionic strength. At an incubation temperature of 30 C, the minimal components were calcium, iron, magnesium, and ammonium ions, thiamine, and a fatty acid source; barium and strontium replaced calcium. Aspartic acid, glutamic acid, or methionine stimulated the rate and amount of growth; the best growth occurred in medium containing additional amino acids. Additions of cyanocobalamin or biotin permitted growth at 37 C. The stimulatory effects of added cyanocobalamin, biotin, pyridoxine, pantothenate, lipoic acid, or nicotinic acid were additive at 37 C, but not at 30 C. Fatty acids containing 14, 16, 17, or 18 carbon atoms supported growth; linoleic and linolenic acids were toxic. Glyceryl monooleate or trioleate, or Tween 40, 60, or 80 supported moderate to good growth; a mixture of monoolein and Tween 60, or Tweens 60 and 80 supported the best growth. Ten strains of L. canicola cultivated in a synthetic medium containing Tweens 60 and 80 attained cellular densities per ml of 10(7) to 4.0 x 10(7) organisms. L. canicola cells, resuspended in medium containing oleic-1-C(14) acid, incorporated label primarily into cellular lipids; a lesser amount was located in the protein fraction, and only trace amounts were found in the nucleic acid fraction. The rate of incorporation was not affected by added sodium acetate. L. canicola was found to have fatty acid decarboxylase activity.

Biotin↗
PubMed1979

The action of tributyltin chloride on the uptake of proline and glutamine by intact cells of Escherichia coli.

Tributyltin chloride inhibits growth and uptake of glutamine and proline into intact cells of Escherichia coli. It causes efflux of the accumulated amino acids. A pH gradient generated in intact cells and everted membrane vesicles is dissipated by this compound. These effects do not require lipoic acid but are dependent on the presence of chloride, bromide, or iodide ions. We conclude that tributyltin chloride can catalyse a transmembrane OH- -anion exchange exchange reaction and that this is its mode of inhibition of the uptake of these amino acids. The response of proline and glutamine uptake to the inhibitor is similar and is consistent with the transport of both amino acids requiring an electrochemical gradient of protons.

Adenosine Triphosphate↗
PubMedDate not supplied

Clinical experience with thioctacid (thioctic acid) in the treatment of distal symmetric polyneuropathy in Korean diabetic patients.

OBJECTIVE: This open-label study was performed to evaluate the efficacy and safety of oral treatment with the antioxidant alpha-lipoic acid (ALA, thioctic acid) in Korean diabetic patients with distal symmetric polyneuropathy (DSP). SUBJECTS AND METHODS: Thioctic acid was administered orally using 600 mg once daily for 8 weeks in 61 diabetic patients with symptomatic polyneuropathy. Neuropathic symptoms (pain, burning sensation, paresthesia, and numbness) were scored at baseline as well as at 4 and 8 weeks following treatment. In addition, neurological assessment was carried out before and after 8 weeks of treatment, and an overall evaluation was performed at the end of treatment. The primary endpoint was the response rate after 8 weeks of treatment, defined as an improvement in the Total Symptom Score (TSS) of > or =30%. RESULTS: Efficacy was evaluated in 38 patients who had completed the study according to the protocol. Safety was evaluated in all 61 patients who had taken the study medication. Fasting blood glucose and HbA(1)c did not change during the study. The response rate after 8 weeks was 71.4%. At 4 weeks, the response rate was 47.4%. The TSS significantly decreased at 4 weeks, which decreased further at 8 weeks (P<.05). All the individual scores for neuropathic symptoms (pain, burning sensation, paresthesia, and numbness) were also significantly reduced at 4 weeks and further decreased at 8 weeks (P<.05). The duration of diabetes, severity and duration of diabetic polyneuropathy, and all the other demographic and metabolic parameters did not demonstrate an effect on the response rate. The parameters of neurological assessment (ankle reflexes, pin-prick test, 10-g monofilament test) and quantitative sensory tests (vibration, warm and cold sensation) were not influenced by 8 weeks of treatment with 600 mg of oral thioctic acid per day. Overall efficacy rated as "good/fair" was 86.8% by the physician and 76.3% by the patients at the end of an 8-week treatment period. Eleven episodes (18.0%) of adverse events (possibly, probably, definitely related) were reported in seven patients (11.5%). CONCLUSION: These findings indicate that oral treatment with thioctic acid at a dose of 600 mg/day for 8 weeks improved symptoms of polyneuropathy in Korean diabetic patients without causing serious adverse events.

Antioxidants↗
PubMed1988

The autoepitope of the 74-kD mitochondrial autoantigen of primary biliary cirrhosis corresponds to the functional site of dihydrolipoamide acetyltransferase.

Autoantibodies to mitochondrial antigens are characteristic of the autoimmune liver disease primary biliary cirrhosis (PBC), but the precise antigenic determinants recognized by these antibodies have not been defined. Recently, our laboratory identified a 1,370-bp rat liver cDNA clone that coded for a polypeptide recognized specifically by sera from patients with PBC but not by sera from patients with other forms of liver disease. This recombinant protein was identified as the 74-kD M2 mitochondrial inner membrane autoantigen, now known to be dihydrolipoamide acetyltransferase. In the present study, we have identified a 603-bp fragment that codes for a polypeptide containing all of the autoreactivity of the original clone. In addition, based on hydrophobicity/hydrophilicity plots of the amino acid sequence of this polypeptide segment, several peptides were synthesized and tested for reactivity by an inhibition assay using sera from patients with PBC. One peptide, defined by the amino acids AEIETDKATIGFEVQEEGYL, absorbed serum reactivity to the protein product of the original clone. Of particular interest was the finding that this peptide contains the lipoic acid binding site KATIGF of the dihydrolipoamide acetyltransferase found in the inner mitochondrial membrane. Thus, it appears that for this autoantigen, the target of the autoantibodies corresponds to a functional site of the dihydrolipoamide acetyltransferase.

Acetyltransferases↗
PubMed2003

Essential 110Cys in active site of membrane-associated prostaglandin E synthase-2.

The amino acid sequence of membrane-associated prostaglandin (PG) E synthase-2 (mPGE synthase-2), which has a broad specificity in its thiol requirement for a catalytic activity, has the consensus region from 104Leu to 120Leu found in glutaredoxin and of thioredoxin. The sequence of Cys-x-x-Cys in the consensus region is the active site for thioredoxin and mPGE synthase-2 also has this amino acid sequence (110Cys-x-x-113Cys). The mutation from 110Cys to Ser or the double mutation from 110Cys and 113Cys to Ser caused loss of PGE synthase activity, whereas the single mutation from 113Cys to Ser did not affect the enzyme activity. These results indicate that 110Cys, but not 113Cys, is the essential amino acid in the active site of mPGE synthase-2. 110Cys is an important amino acid in PGE synthase activity and plays the critical role as Cys at the same position in redoxin. Moreover, we found that the reduced form of lipoic acid (dihydrolipoic acid) serves as one of the natural activators of mPGE synthase-2 in the cells.

Amino Acid Sequence↗
PubMed1992

Purification, characterization and function of dihydrolipoamide dehydrogenase from the cyanobacterium Anabaena sp. strain P.C.C. 7119.

A dihydrolipoamide dehydrogenase (dihydrolipoamide: NAD+ oxidoreductase, EC 1.8.1.4) (DLD) has been found in the soluble fraction of cells of both unicellular (Synechococcus sp. strain P.C.C. 6301) and filamentous (Calothrix sp. strain P.C.C. 7601 and Anabaena sp. strain P.C.C. 7119) cyanobacteria. DLD from Anabaena sp. was purified 3000-fold to electrophoretic homogeneity. The purified enzyme exhibited a specific activity of 190 units/mg and was characterized as a dimeric FAD-containing protein with a native molecular mass of 104 kDa, a Stokes' radius of 4.28 nm and a very acidic pI value of about 3.7. As is the case with the same enzyme from other sources, cyanobacterial DLD showed specificity for NADH and lipoamide, or lipoic acid, as substrates. Nevertheless, the strong acidic character of the Anabaena DLD is a distinctive feature with respect to the same enzyme from other organisms. The presence of essential thiol groups was suggested by the inactivation produced by thiol-group-reactive reagents and heavy-metal ions, with lipoamide, but not NAD+, behaving as a protective agent. The function and physiological significance of Anabaena DLD are discussed in relation to the fact that 2-oxoacid dehydrogenase complexes have not been detected so far in filamentous cyanobacteria. Glycine decarboxylase activity, which might be involved in photorespiratory metabolism, has been found, however, in cell extracts of Anabaena sp. strain P.C.C. 7119 as the present study demonstrates.

Amino Acid Oxidoreductases↗
PubMed2000

Insulin resistance: lifestyle and nutritional interventions.

Insulin resistance appears to be a common feature and a possible contributing factor to several frequent health problems, including type 2 diabetes mellitus, polycystic ovary disease, dyslipidemia, hypertension, cardiovascular disease, sleep apnea, certain hormone-sensitive cancers, and obesity. Modifiable factors thought to contribute to insulin resistance include diet, exercise, smoking, and stress. Lifestyle intervention to address these factors appears to be a critical component of any therapeutic approach. The role of nutritional and botanical substances in the management of insulin resistance requires further elaboration; however, available information suggests some substances are capable of positively influencing insulin resistance. Minerals such as magnesium, calcium, potassium, zinc, chromium, and vanadium appear to have associations with insulin resistance or its management. Amino acids, including L-carnitine, taurine, and L-arginine, might also play a role in the reversal of insulin resistance. Other nutrients, including glutathione, coenzyme Q10, and lipoic acid, also appear to have therapeutic potential. Research on herbal medicines for the treatment of insulin resistance is limited; however, silymarin produced positive results in diabetic patients with alcoholic cirrhosis, and Inula racemosa potentiated insulin sensitivity in an animal model.

Complementary Therapies↗
PubMed1975

Co-oxygenation of organic substrates by the prostaglandin synthetase of sheep vesicular gland.

The microsomal fraction of sheep vesicular glands has been found to oxygenate 1,3-diphenylisobenzofuran, luminol, and the carcinogenic hydrocarbon benzopyrene when incubated with arachidonic acid. The oxygenations demonstrate an absolute dependence on enzyme and fatty acid and can be completely inhibited by indomethacin and 2,3-dimercaproptopanol, inhibitors of prostaglandin synthetase. The oxygenations can also be stimulated by the hydroperoxy endoperoxide, prostaglandin G2, and 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid. These latter reactions are not inhibited by indomethacin or dimercaptopropanol but do require the microsomal enzyme system. The involvement of superoxide anion in the transformations could not be demonstrated. The oxygenations occurring in the presence of arachidonic acid appear to arise via the interaction of a microsomal enzyme system with hydroperoxide intermediates of prostaglandin biosynthesis. The ability of various sulfur reagents (reduced glutathione, alpha-lipoic acid, methional) to inhibit co-oxygenation is probably related to their ability to stimulate the conversion of the intermediate to prostaglandins.

Animals↗
PubMedDate not supplied

[Dependence of [14C] nicotinate and [35S] lipoate transport to erythrocytes on their Mg2+, Na+, K+-ATPase activity].

Nicotinic acid added to the incubation medium stimulates ATPase activity in erythrocytes and their membranes. Simultaneously the ouabain-sensitive ATPase activity is activated. The mentioned effect is not observed when lipoic acid is added to the medium. Accumulation of [14C]nicotinate and [35S]lipoate in biostructures occurs more intensely under conditions optimal for the Mg2+, Na+, K+-ATPase activity. In experiments with "traces" of erythrocytes it is shown that the gradient of Na+ and K+ favours to the transport of [35S] lipoate.

Animals↗
PubMed1976

Selective inactivation of the transacylase components of the 2-oxo acid dehydrogenase multienzyme complexes of Escherichia coli.

1. The reaction of the pyruvate dehydrogenase multienzyme complex of Escherichia coli with maleimides was examined. In the absence of substrates, the complex showed little or no reaction with N-ethylmaleimide. However, in the presence of pyruvate and N-ethylmaleimide, inhibition of the pyruvate dehydrogenase complex was rapid. Modification of the enzyme was restricted to the transacetylase component and the inactivation was proportional to the extent of modification. The lipoamide dehydrogenase activity of the complex was unaffected by the treatment. The simplest explanation is that the lipoyl groups on the transacetylase are reductively acetylated by following the initial stages of the normal catalytic cycle, but are thereby made susceptible to modification. Attempts to characterize the reaction product strongly support this conclusion. 2. Similarly, in the presence of N-ethylmaleimide and NADH, much of the pyruvate dehydrogenase activity was lost within seconds, whereas the lipoamide dehydrogenase activity of the complex disappeared more slowly: the initial site of the reaction with the complex was found to be in the lipoyl transacetylase component. The simplest interpretation of these experiments is that NADH reduces the covalently bound lipoyl groups on the transacetylase by means of the associated lipoamide dehydrogenase component, thereby rendering them susceptible to modification. However, the dependence of the rate and extent of inactivation on NADH concentration was complex and it proved impossible to inhibit the pyruvate dehydrogenase activity completely without unacceptable modification of the other component enzymes. 3. The catalytic reduction of 5,5'-dithiobis-(2-nitrobenzoic acid) by NADH in the presence of the pyruvate dehydrogenase complex was demonstrated. A new mechanism for this reaction is proposed in which NADH causes reduction of the enzyme-bound lipoic acid by means of the associated lipoamide dehydrogenase component and the dihydrolipoamide is then oxidized back to the disulphide form by reaction with 5,5'-dithiobis-(2-nitrobenzoic acid). 4. A maleimide with a relatively bulky N-substituent, N-(4-diemthylamino-3,5-dinitrophenyl)maleimide, was an effective replacement for N-ethylmaleimide in these reactions with the pyruvate dehydrogenase complex. 5. The 2-oxoglutarate dehydrogenase complex of E. coli behaved very similarly to the pyruvate dehydrogenase complex, in accord with the generally accepted mechanisms of the two enzymes. 6. The treatment of the 2-oxo acid dehydrogenase complexes with maleimides in the presence of the appropriate 2-oxo acid substrate provides a simple method for selectively inhibiting the transacylase components and for introducing reporter groups on to the lipoyl groups covalently bound to those components.

Disulfides↗
PubMed1989

Primary biliary cirrhosis: current knowledge, perspectives, and future directions.

These perspectives from the first International Symposium on Primary Biliary Cirrhosis review recent advances and single out some areas for further enquiry. The latter include frequency and type of associated autoimmune diseases, the existence of clinical subsets of PBC, immunohistochemical analysis of lymphoid infiltrates in the liver, effects of immunosuppressive and other treatment regimens, and models for predicting the optimal time for liver transplantation. The M2 autoantigens have been identified as mitochondrial 2-oxo-acid dehydrogenase enzymes. These include pyruvate dehydrogenase (70-74 kd antigen) and branched chain 2-oxo-acid dehydrogenase and 2-oxo-acid glutaric dehydrogenase (45-52 kd antigens). Each of these enzymes has three subunits, E1 to E3. For PDH, an autoepitope has been identified as a decapeptide containing the attachment site of lipoic acid, an essential cofactor for enzyme activity. Current questions include the degree to which antibodies to PDH, and related enzymes, account for the mitochondrial reactivity defined by immunofluorescence or other procedures, the cell-surface expression of M2 autoantigens, and the significance of the occurrence of nonmitochondrial (such as centromeric) autoantibodies in PBC. The unknown T lymphocyte contribution to the autoimmune response in PBC may involve inducer and effector components. A postulated T-cell autoepitope may be presented, in association with MHC class I or class II molecules, on the surface of biliary epithelial cells. T cell lines from PBC livers removed during transplantation could provide data on the T-lymphocyte contribution to the pathogenesis of PBC.

Humans↗
PubMed1982

Nutritional requirements of Corynebacterium pyogenes.

The nutritional requirements of Corynebacterium pyogenes (strains C100, 5, and 1909), a commonly encountered animal pathogen, were determined in this study. A semidefined medium (SDM) containing glucose, HCO3-, hemin, charcoal-treated Trypticase, and a defined mixture of purines and pyrimidines, amino acids, and minerals which supported optimal growth of C. pyogenes was employed in all nutritional studies. Adenine and uracil were required for optimal growth of strains 5 and C100 but were not required for strain 1909. Riboflavin and nicotinic acid were required for good growth of all three strains; biotin and thiamin were stimulatory but did not appear to be required for growth. Hemin and NaHCO3 were stimulatory for growth, whereas lipoic acid and Tween 80 were neither stimulatory nor required for growth. The replacement of Trypticase with a specific peptide fraction (obtained by fractionation of Trypticase on Sephadex G-25) rich in dipeptides gave growth comparable to that in SDM, indicating a peptide requirement for the growth of C. pyogenes. It was of considerable interest that growth comparable to that in SDM was obtained when Trypticase was replaced by inositol (1 microgram/ml of SDM).

Amino Acids↗
PubMed1993

Dihydrolipoic acid protects pancreatic islet cells from inflammatory attack.

In vitro models of pancreatic islet cell inflammation are the lysis of isolated islet cells by activated macrophages or by oxygen radicals released by the endothelial enzyme xanthine oxidase. Dihydrolipoic acid protected islet cells in both systems by different modes of action. Macrophage cytotoxicity towards islet cells, which is nitric-oxide-mediated, was suppressed by 2 h of preincubation of macrophages with lipoic acid. Similarly, 2 h of preincubation sufficed to protect islet cells against enzymatically produced oxygen radicals. Dihydrolipoic acid was found by chemiluminescence assay to scavenge directly such radicals. In macrophages dihydrolipoic acid suppressed the production of nitrite as a measure of nitric oxide release. These results suggest that dihydrolipoic acid is an anti-inflammatory agent which at the same time interferes with nitric oxide release from inflammatory macrophages and protects target cells from oxygen radical attack.

Animals↗
PubMed2003

Copper toxicity, oxidative stress, and antioxidant nutrients.

Copper (Cu) is an integral part of many important enzymes involved in a number of vital biological processes. Although normally bound to proteins, Cu may be released and become free to catalyze the formation of highly reactive hydroxyl radicals. Data obtained from in vitro and cell culture studies are largely supportive of Cu's capacity to initiate oxidative damage and interfere with important cellular events. Oxidative damage has been linked to chronic Cu-overload and/or exposure to excess Cu caused by accidents, occupational hazards, and environmental contamination. Additionally, Cu-induced oxidative damage has been implicated in disorders associated with abnormal Cu metabolism and neurodegenerative changes. Interestingly, a deficiency in dietary Cu also increases cellular susceptibility to oxidative damage. A number of nutrients have been shown to interact with Cu and alter its cellular effects. Vitamin E is generally protective against Cu-induced oxidative damage. While most in vitro or cell culture studies show that ascorbic acid aggravates Cu-induced oxidative damage, results obtained from available animal studies suggest that the compound is protective. High intakes of ascorbic acid and zinc may provide protection against Cu toxicity by preventing excess Cu uptake. Zinc also removes Cu from its binding site, where it may cause free radical formation. Beta-carotene, alpha-lipoic acid and polyphenols have also been shown to attenuate Cu-induced oxidative damage. Further studies are needed to better understand the cellular effects of this essential, but potentially toxic, trace mineral and its functional interaction with other nutrients.

Animals↗
PubMed1994

The fabJ-encoded beta-ketoacyl-[acyl carrier protein] synthase IV from Escherichia coli is sensitive to cerulenin and specific for short-chain substrates.

A fourth fatty acid condensing enzyme was isolated from Escherichia coli by its ability to restore elongating activity to a protein extract which had been treated with cerulenin, a condensing enzyme-specific inhibitor. The purified beta-ketoacyl-[acyl carrier protein] (ACP) synthase IV [3-oxoacyl-ACP synthase; acyl-ACP:malonyl-ACP C-acyltransferase (decarboxylating), EC 2.3.1.41] (KAS IV) is specific for short-chain acyl-ACP substrates. The enzyme is stable at 43 degrees C and very sensitive to cerulenin (50% inhibition at 3 microM), which binds covalently. A condensing enzyme-specific antibody raised to an expressed open reading frame from barley was used to identify KAS IV protein in Western blots, and the sequence obtained for 30 amino-terminal residues. This led to the isolation of the fabJ gene located in the fab cluster at 24.8 min of the E. coli chromosome. The fabJ gene encodes a polypeptide of 413 amino acids and molecular mass 43 kDa that shows 38% identity and 64% similarity to the fabB-encoded KAS I. The amino acid sequence of KAS IV, however, is more similar to all other published condensing enzyme sequences than the KAS I sequence is. A specialized putative function for this enzyme is to supply the octanoic substrates for lipoic acid biosynthesis. We predict that an analogue of KAS IV with the same function will be found in plant mitochondria. The described complementation assay can be used to detect condensing enzymes with other substrate specificities by supplementing the cerulenin-treated extract with appropriate purified KAS enzymes.

3-Oxoacyl-(Acyl-Carrier-Protein) Synthase↗
PubMed1999

Detection of anti-branched chain 2-oxo acid dehydrogenase complex (BCOADC)-E2 antibody in primary biliary cirrhosis by ELISA using recombinant fusion protein.

Anti-M2 of anti-mitochondrial antibody (AMA) is a serological marker of primary biliary cirrhosis (PBC). Anti-pyruvate dehydrogenase complex-E2 (anti-PDC-E2) is recognized as the most frequently occurring anti-M2, and a routine laboratory test for this antibody has already been established. However, it is also known that there are patients with PBC who are negative for anti-PDC-E2. For the serological diagnosis of these patients, immunoblotting for anti-M2s is indicated. However, the technique currently utilized is too laborious to allow testing of a large number of samples. In this study, we have developed an enzyme-linked immunosorbent assay (ELISA) using a recombinant fusion protein in order to evaluate anti-branched chain 2-oxo-acid dehydrogenase complex-E2 (anti-BCOADC-E2), another frequently occurring anti-M2 in PBC patients. KB cell lines (CCL 17) were utilized as source material, and BCOADC-E2 cDNA (971 bp) including the lipoic acid binding domain was amplified by polymerase chain reaction. The amplified region was subcloned into pEX-3 vectors and expressed, and the resulting fusion protein (beta-galactosidase/BCOADC-E2) was utilized as antigen for an ELISA. We ascertained the specificity of this antigen by inhibition tests with ELISA and immunoblotting. We defined the cut-off optical density (OD) value as the mean + 3 SD (0.146) of sera from 60 normal controls. Anti-BCOADC-E2 could not be detected with this assay in sera from normal controls and from patients with autoimmune hepatitis and chronic viral hepatitis. Anti-BCOADC-E2 was detected in 119 of 210 sera (56.7%) from patients with PBC. In addition, anti-BCOADC-E2 was detected in 48 of 99 (48.5%) sera from PBC patients who were negative for anti-PDC-E2. Here, we have succeeded in developing a new ELISA for detecting anti-BCOADC-E2. This system is antigen-specific and easily performed. This assay should allow routine testing of a large number of serum samples, and should become especially useful for the serodiagnosis of anti-PDC-E2-negative PBC patients.

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)↗
PubMed1990

Inhibition of poly(ADP-ribose) synthetase by unsaturated fatty acids, vitamins and vitamin-like substances.

Various vitamins and vitamin-like substances inhibited the activity of poly(ADP-ribose) synthetase in vitro. The most potent were essential fatty acids, i.e. arachidonic acid, linoleic acid, and linolenic acid; their 50% inhibitory concentrations (IC50) were 44-110 microM, indicating a higher potency than nicotinamide, a well-known vitamin inhibitor (IC50 = 210 microM). Vitamins K3, K1, and retinal were the next strongest inhibitors, followed by alpha-lipoic acid, coenzyme Q0, and pyridoxal 5-phosphate. Nicotinamide and vitamin K3 exhibited mixed-type inhibition with respect to NAD+, while arachidonic acid exhibited dual inhibitions, competitive at 50 microM and mixed-type at 100 microM.

Animals↗
PubMed1961

Growth of Listeria monocytogenes in defined media.

Friedman, Mischa E. (U. S. Army Chemical Corps, Fort Detrick, Frederick, Md.), and William G. Roessler. Growth of Listeria monocytogenes in defined media. J. Bacteriol. 82:528-533. 1961-Listeria monocytogenes, strains A4413, JHH, and 9037-7, require organic sulfur, valine, and isoleucine for growth. In addition, A4413 requires leucine, whereas 9037-7 requires leucine, histidine, and arginine. Glutamine is stimulatory for all three strains. Further, A4413 is stimulated also by histidine, arginine, and methionine, and JHH by histidine, arginine, and leucine. With A4413, glutamine can be replaced by inorganic ammonium salts, urea, or asparagine but not by glutamic acid. Growth inhibition by d-serine is reversed by glycine or alanine. Growth with agitation in defined media is very poor and subculture is not possible unless unidentified products of enzymatic hydrolysis of proteins are present.A requirement for lipoic acid was not observed with five strains of L. monocytogenes.

Alanine↗