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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cell walls were isolated by mechanical disruption of mid-log phase cells of Bacillus stearothermophilus NCA 1503-4R grown in Trypticase-yeast extract-fructose medium at 55 C. The cell walls were purified by treatment with sodium dodecyl sulfate (SDS) and incubation with deoxyribonuclease and trypsin. The cell wall peptidoglycan contained glucosamine, muramic acid, alpha, epsilon-diaminopimelic acid, and glutamic acid. Low amounts of glycine, galactosamine, serine, aspartic acid, lysine, and valine were also present. The relative mole ratios of glutamic acid-alpha, epsilon-diaminopimelic acid-glycine-alanine were 1.00:1.26:0.08:1.55. The cell walls were free from ribonucleic acid and deoxyribonucleic acid and contained less than 0.2% chloroform-methanol extractable lipid and 0.09 mumole of phosphorus per mg of cell wall. Teichoic acid was not detected in the cell walls of this organism. Cell walls isolated without treatment with SDS contained 7.5% chloroform-methanol extractable lipid, 0.24 mumole of phosphorus per mg of cell wall, and relatively high concentrations of all amino acids. These results suggest that the extracted lipid is not a cell wall component per se, but a contaminant from the lipoprotein cell membrane.
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PMID:Chemical composition of the cell walls of Bacillus stearothermophilus. 603 16

The mechanism of ammonia assimilation in Methanosarcina barkeri and Methanobacterium thermoautotrophicum was documented by analysis of enzyme activities, 13NH3 incorporation studies, and comparison of growth and enzyme activity levels in continuous culture. Glutamate accounted for 65 and 52% of the total amino acids in the soluble pools of M. barkeri and M. thermoautotrophicum. Both organisms contained significant activities of glutamine synthetase, glutamate synthase, glutamate oxaloacetate transaminase, and glutamate pyruvate transaminase. Hydrogen-reduced deazaflavin-factor 420 or flavin mononucleotide but not NAD, NADP, or ferredoxin was used as the electron donor for glutamate synthase in M. barkeri. Glutamate dehydrogenase activity was not detected in either organism, but alanine dehydrogenase activity was present in M. thermoautotrophicum. The in vivo activity of the glutamine synthetase was verified in M. thermoautotrophicum by analysis of 13NH3 incorporation into glutamine, glutamate, and alanine. Alanine dehydrogenase and glutamine synthetase activity varied in response to [NH4+] when M. thermoautotrophicum was cultured in a chemostat with cysteine as the sulfur source. Alanine dehydrogenase activity and growth yield (grams of cells/mole of methane) were highest when the organism was cultured with excess ammonia, whereas growth yield was lower and glutamine synthetase was maximal when ammonia was limiting.
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PMID:Ammonia assimilation and synthesis of alanine, aspartate, and glutamate in Methanosarcina barkeri and Methanobacterium thermoautotrophicum. 612 78

Human liver alanine aminopeptidase (EC 3.4.11.14; L-alpha-aminoacyl-peptide hydrolase) catalyzes the stepwise hydrolysis of methionyl-lysyl-bradykinin to yield methionine, lysine, and the limit nonapeptide, bradykinin which is resistant to further hydrolytic cleavage by this enzyme. Alanine aminopeptidase also catalyzes the hydrolysis of various neutral amino acid beta-naphthylamides. This enzyme cleaves N-terminal arginyl residues unless the adjacent penultimate residue is proline as is the case for bradykinin. The properties are consistent with the requirements of a kinin converting enzyme. Human alanine aminopeptidase activity is reduced by several beta-lactam antibiotics, with the cloxacillin, oxacillin, and methicillin Ki values being 0.51 mM, 1.6 mM, and 2.4 mM respectively. Our experiments with radioactively labelled penicillin indicate that two moles of antibiotic are bound per mole of enzyme. Neither chromatography of the penicillin-treated enzyme on G-25 Sephadex, treatment of penicillin-G-treated enzyme with penicillinase, nor extensive dilution of cloxacillin-treated enzyme diminished the degree of inactivation produced. Inhibition was obtained with 6-aminopenicillanic acid, which indicated that the penicillin nucleus itself was being bound, but substitutions, as in cloxacillin, could enhance the binding.
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PMID:Human-liver alanine aminopeptidase. A kinin-converting enzyme sensitive to beta-lactam antibiotics. 612 21

The solution spinning of a random copolypeptide of gamma-benzyl-L-glutamate polymerized with L-alanine at a mole ratio of 1 to 4 has been examined. Good fibers were obtained by using dichloroacetic acid and water as solvent and coagulation reagent respectively. The mechanical properties of the fibers are comparable with those of natural fibers.
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PMID:Spinning of a random copolypeptide composed of gamma-benzyl-L-glutamate and L-alanine. 615 20

Seven strains of Rothia dentocariosa were degraded by acid methanolysis and the nonhydroxylated fatty acid methyl esters released were examined by thin-layer and gas chromatography. The fatty acid profiles were composed of iso-, anteiso- and straight chain saturated fatty acids with 12-methyltetradecanoic (anteiso-C15), 14-methylpentadecanoic (iso-C16), 14-methylhexadecanoic (anteiso-C17) and hexadecanoic acid (C16) as major components. A small scale integrated procedure was used for the sequential extraction of isoprenoid quinones and polar lipids. The latter were examined by two-dimensional thin-layer chromatography and all of the test strains contained diphosphatidylglycerol, phosphatidylglycerol and two uncharacterised glycolipids. In all cases the major isoprenoid quinones were unsaturated menaquinones with seven isoprene units. Analyses of the cell wall amino acid composition using gas chromatography showed that the strains contained 2.5 to 5 moles of alanine and 1 mole each of glutamic acid and lysine. The chemical data support the integrity of Rothia dentocariosa and can be used to separate it from all other actinomycetes especially those which contain lysine in the wall peptidoglycan.
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PMID:Lipid and wall amino acid composition in the classification of Rothia dentocariosa. 648 31

The content and D-alanyl ester complement of lipoteichoic acid from stationary-phase culture filtrates of Streptococcus mutans (strains BHT and GS-5; serotypes b and c) were determined chemically and serologically. A third less lipoteichoic acid was obtained from strain GS-5 than from strain BHT. This lipoteichoic acid had an increased mobility on immunoelectrophoresis after exposure overnight at pH 8 and a 10-fold greater content of alanine per mole of glycerol.
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PMID:D-Alanyl-substituted glycerol lipoteichoic acid in culture fluids of Streptococcus mutans strains GS-5 and BHT. 650 Jul 17

Extensive succinylation of 19 S normal human thyroglobulin having a high iodine content results in the formation of a 26,000-Da peptide. One-half mole of the peptide is obtained from 1 mol of the high molecular weight glycoprotein. The dissociation of the peptide is accompanied by the appearance of an intense absorption band which has a maximum at 264 nm. The absorption band is associated exclusively with the 26,000-Da peptide. The amino acid composition of the peptide differs from 19 S thyroglobulin by having no cysteine and higher contents of serine, alanine, tyrosine, phenylalanine, lysine, glycine, isoleucine, and histidine. The peptide also has a high thyroxine content. There were no detectable carbohydrates in the peptide. The fluorescence spectrum of the 26,000-Da peptide shows an emission maximum at 405 nm which we have recently assigned to iodotyrosine-iodotyrosine interactions (Shifrin, S., Consiglio, E., and Kohn, L. D. (1983) J. Biol. Chem. 258, 3780-3786). A 26,000-Da peptide with the same physicochemical properties is found in extracts of normal human thyroid glands.
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PMID:Noncovalent interactions of a 26,000-dalton peptide with 19 S human thyroglobulin. 663 Feb

1. The kinetic parameters of lysine and alanine uptake by rabbit ileal mucosa have been measured in the presence and absence of Na. 2. Using lysine as an inhibitor of part of alanine uptake in the absence of Na it has been possible to define two mediated systems for alanine entry. One of these systems (Km 14.2 mM; Jmax 41.3 n-mole cm-2 min-1) is inhibited by lysine (Ki 0.96 mM) while the other (Km 115 mM; Jmax 323 n-mole cm-2 min-1) is not. 3. Methionine is an effective inhibitor of both Na-independent uptake mechanisms for alanine. 4. Na-independent lysine uptake also takes place through two mediated systems. One of these systems (Km 1.0 mM; Jmax 12.8 n-mole cm-2 min-1) is inhibited by alanine (Ki 4.3 mM) while the other (Km 108 mM; Jmax 194 n-mole cm-2 min-1) is not. 5. The use of a naturally occurring basic amino acid to inhibit a portion of neutral amino acid uptake extends considerably the ability to distinguish multiple acid transport systems present in the same cell membrane. The physiological implications of these findings are discussed.
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PMID:Distinguishing transport systems having overlapping specificities for neutral and basic amino acids in the rabbit ileum. 679 99

1. In the goldfish retina, uptake of exogenous [3H]glycine follows Michaelis--Menten kinetics with increasing concentrations of glycine. This uptake can be explained kinetically by the presence of two independent affinity systems: a 'high-affinity' mechanism with an apparent Km(H) of 8.1 microM and a Vmax(H) of 9.12 p-moles/min. mg protein, and a 'low-affinity' mechanism with an apparent Km(L) of 0.63 mM and a Vmax(L) of 430 p-mole/min . mg protein. 2. The high-affinity mechanism, and probably also the low-affinity mechanism, is temperature- and Na+-dependent. 3. The low-affinity mechanism for glycine uptake is not affected by 5 mM-isoleucine, methionine and valine in the medium. However, it is inhibited more than 90% by 5 mM-alanine, proline and serine in the medium. This result indicates that the low-affinity transport for glycine may go through system A of the neutral amino acid transport system which is present in most tissues to transport glycine and certain neutral amino acids for metabolic purposes. 4. The high-affinity mechanism for glycine uptake is, however, not affected by the presence of up to 100-fold excess of all amino acids examined. 5. Autoradiographic studies show that at least one type of amacrine cell and one type of probable interplexiform cell take up [3H]glycine both in the presence and absence of 5 mM-alanaine, proline and serine, indicating that these neurones possess the high-affinity mechanism for glycine uptake. 6. [3H]Glycine accumulated in the retina can be released by increasing the external K+ concentration. This release is probably Ca2+-dependent since it is blocked by 10 mM-Co2+ in the medium. Additionally, autoradiographic studies show that [3H]glycine taken up by the glycine-accumulating neurones can also be released by Ca2+-dependent, K+-depolarization of the retina.
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PMID:The uptake and release of [3H]glycine in the goldfish retina. 723 15

Two fractions of human prothrombin can be isolated from single donor plasma by the technique of heparin-agarose chromatography in (sodium) citrate buffer, pH 7.5, as previously reported for pooled plasma. The two fractions, designated H-II1 and H-II2, are found in a ratio of approximately 4:1. Both forms comigrate in sodium dodecyl sulfate gel electrophoresis; however, under nondenaturing electrophoretic conditions, each fraction migrates as a discrete entity with a different mobility. The larger fraction (H-II1) has a faster mobility towards the anode. Isoelectric focusing in urea of H-II1 reveals that it has two components, a minor component with a pl of 5.25 (H-II1a) and a major component with a pl of 5.40 (H-II1b). H-II2 has a pl of 5.6 H-II1 and H-II2 possess the same amino terminal residue (alanine, 0.87-0.92 mole/mole) and the same number of gamma -carboxyglutamic acid residues (9.8-10.5). Their amino acid composition is indistinguishable. However, the two fractions of prothrombin differ in their content of neutral sugar and of sialic acid residues. Removal of sialic acid with neuraminidase abolishes the electrophoretic heterogeneity. Thus, the charge heterogneity of the three variants of prothrombin found in normal human plasma appears to result exclusively from differences in the number of sialic acid residues attached to the protein moiety of the molecule.
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PMID:Heterogeneity in human prothrombin: analysis of cause. 729


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