Dynamics of amino acids in the conditioning film developed on glass panels immersed in the surface seawaters of Dona Paula Bay

The conditioning film developed on glass panels immersed in surface seawater over a period of 24?h was analysed for total organic carbon (OC), total organic nitrogen (ON), and total hydrolyzable amino acid (THAA) concentrations and composition. The concentrations of C and N and THAA increased, whereas the C/N ratio decreased over the period of immersion. The amino acid-C and N accounted for 3.7?–?6.7% and 10.3?–?65.3% of OC and ON, respectively. The relative contribution of glycine plus threonine and serine to the total amino acids decreased while that of valine, phenylalanine, isoleucine and leucine increased over the period of immersion. Principal component analysis (PCA) based on mole% amino acid composition showed that the degradation indices (DI) for the conditioning film organic matter increased over the period of immersion. A high C/N ratio, a low %THAA-C, % THAA-N and DI values and the abundance of glycine plus threonine and serine in the conditioning film organic matter during the first few hours following immersion imply that the adsorbed organic matter was mostly derived from degraded organic matter.     

Fluxes of diatoms in the Dona Paula Bay, west coast of India

Sediment traps were deployed at a station in the Dona PaulaBay to collect sedimenting particles at weekly intervals fromNovember to May during 1995–1997. Sedimented particleswere analysed for total diatom flux, chlorophyll a (Chl a) andparticulate organic carbon (POC). The highest diatom flux wasrecorded in April–May for both the years. Fluxes of diatomsvaried from0.6 x 10⁴ cells m^–2 day^–1 (November 1995)to 121.47 x 10⁴ cells m^–2 day^–1 (December 1996).In all, 19 diatom genera were identified in the sedimented material.Navicula, Nitzschia, Pleurosigma, Licmophora, Coscinodiscus,Rhizosolenia and Surirella were the most abundant genera inthe sedimented material throughout the sampling period. Meanflux of POC and diatom carbon was 251 and 0.39 mg C m^–2day^–1, respectively. The diatom carbon accounted for 0.15%of the POC flux. Mass flux of diatoms showed significant negativecorrelation with the concentration of nitrate and phosphate.This suggests that the nutrient concentration played an importantrole in influencing the sedimentation of diatoms at this coastalstation.     

Kinetics of conditioning layer formation on stainless steel immersed in seawater

Adhesion of microorganisms to surfaces in marine environments leads to biofouling. The deleterious effects of biofilm growth in the marine environment are numerous and include energy losses due to increased fluid frictional resistance or to increased heat transfer resistance, the risk of corrosion induced by microorganisms, loss of optical properties, and quality control and safety problems. Antifouling agents are generally used to protect surfaces from such a biofilm. These agents are toxic and can be persistent, causing harmful environmental and ecological effects. Moreover, the use of biocides and regular cleaning considerably increase the maintenance costs of marine industries. An improved knowledge of bio‐film adhesion mechanisms is needed for the development of an alternative approach to the currently used antifouling agents. The aim of this study is to characterise the chemical composition of the molecules first interacting with stainless steel during the period immediately following immersion in natural seawater and to elucidate the kinetics of the adsorbtion process. Proteins are shown to adhere very rapidly, closely followed by carbohydrates. The distribution on the surface of organic molecules is also examined. The ad‐sorbate on the surface is not a continuous film but a heterogeneous deposit, whose average thickness varies widely. The cleaning procedures used affect the adsorption kinetics. In particular, cleaning with hexane results in slower adsorption of nitrogen‐containing species than does cleaning in acetone.     

Dynamics of the ion cyclotron resonance effect on amino acids adsorbed at the interfaces

In this study we show a reproduction of the Zhadin experiment, which consists of the transient increase of the electrolytic current flow across an aqueous solution of L-arginine and L-glutamic acid induced by a proper low frequency alternating magnetic field superimposed to a static magnetic field of higher strength. We have identified the mechanisms that were at the origin of the so-far poor reproducibility of the above effect: the state of polarization of the electrode turned out to be a key parameter. The electrochemical investigation of the system shows that the observed phenomenon involves the transitory activation of the anode due to ion cyclotron frequency effect, followed again by anode passivation due to the adsorption of amino acid and its oxidation products. The likely occurrence of similar ion cyclotron resonance (ICR) phenomena at biological membranes, the implications on ion circulation in living matter, and the consequent biological impact of environmental magnetic fields are eventually discussed.     

Dynamics of free amino acids in rat brain tissue during hypothermia

A comparative study is conducted for the effect of one-, three- and six-hour artificial deep (20-19 degrees C) hypothermia on the content of free amino acids in the blood serum, tissue, nuclei and mitochondria of the rat brain. It is found out that the content is the highest in the blood serum after a three-hour cooling. In the brain tissue the amount of amino acids lowers, especially under conditions of a six-hour hypothermia. In nuclei a three-hour effect of hypothermia decreases sharply the content of free amino acids and the six-hour one increases the amount of most of them. Under hypothermia the content of nearly all amino acids in the brain mitochondria is higher than in the intact animals.     

Quantitative gas chromatographic analysis of amino acids on a short glass capillary column

A study of the quantitative gas chromatographic analysis of protein amino acids as their N-heptafluorobutyric amino acid n-propyl esters on a glass capillary column has been made. The analysis is completed within 35 min with good separation of the common protein amino acids in a single-column run.Hydrolyzed peptides have been analyzed. The analyses were performed with a precision varying between 1 and 6% (mean relative standard deviation) depending on the number of amino acid residues in the peptide. The amount taken for analysis was 20–300 μg. The results agree with the known sequences of the peptides and with the analyses by ion-exchange chromatography except for cysteine. This amino acid can be analyzed after modification as S-methylated cysteine.     

Analysis of thiohydantoins from amino acids by gas-liquid chromatography on short glass capillary columns

A method for separation of amino acid methyl or phenyl thiohydantoins by GLC on a short glass capillary column is described. Calculations of required parameters of the capillary column are presented. By the described methods, nineteen of twenty silylated methylthiohydantoins were separated in one run. The last one (histidine) can be identified on the same column by starting the analysis at a higher temperature. Cysteine and arginine were analysed as S-methylcysteine and ornithine, respectively.     

Differential microbial uptake of dissolved amino acids and amino sugars in surface waters of the Atlantic Ocean

Nitrogen bioavailability is considered to limit the productivityof oceanic oligotrophic gyres, the largest biomes on Earth.In order to assess the microbial requirement for small organicnitrogen molecules in these and other waters, the microbialuptake rates of amino acids (leucine, methionine and tyrosine)and amino sugars (glucosamine and N-acetyl-glucosamine) as wellas glucose were compared using a bioassay technique of radiotracerdilution. The bioassays were carried out on four mid-Atlanticmeridional transects spanning a latitudinal range from 60°Nto 42°S. The mean concentrations of both bioavailable N-acetyl-glucosamineand glucose in the gyres were 1 nM, four times higher than themean leucine concentration. Despite its lower concentration,the mean turnover time of leucine in the gyres of 15 h was 90and 9 times shorter than the turnover time of N-acetyl-glucosamineand glucose, respectively. In addition, among amino acids, leucinewas taken up in the gyres at a rate of 1.5 times faster thanmethionine and 2.5 times faster than tyrosine. Hence, oceanicbacterioplankton as a community showed a clear preference foramino acids, particularly leucine, compared with amino sugars.The preferential uptake of amino acids to sugars challengesthe concept of microbial nitrogen or carbon limitation in theopen ocean.     

Effects of branched-chain amino acids on plasma amino acids in amyotrophic lateral sclerosis

Summary Although the cause of amyotrophic lateral sclerosis (ALS) remains unknown, biological findings suggest that the excitatory amino acid glutamate contributes to the pathogenesis of ALS. In previous studies of ALS, the therapeutic effect of the branched-chain amino acids (BCAAs) leucine, valine and isoleucine has been evaluated. The present study aimed at investigating the acute effect of BCAAs on plasma glutamate levels in ALS patients. Following two oral doses of BCAAs, significantly increased plasma levels were seen for valine (500%), isoleucine (1,377%) and leucine (927%), however the plasma level of glutamate was not affected. The plasma level of several other amino acids (tryptophan, tyrosine, phenylalanine and methionine) were found decreased after oral BCAAs, which may indicate a diminution in the rate of degradation of muscle protein and/or an increase in tissue disposal of amino acids.     

Rapid separation of phenylthiohydantoin (PTH) amino acids by thin-layer chromatography on polyamide glass plates

1.

1. A rapid and sensitive method is described for the two-dimensional separation of 24 PTH derivatives by thin-layer chromatography on commercially available polyamide glass plates. This method gives 21 to 22 unique spots by combination of the solvent systems applied.     

Studies on the decomposition of amino acids in soils

Summary 1. Anaerobic amino-acid breakdown in a garden soil was accompanied by the formation of large quantities of volatile fatty acid and ammonia (plus indole in the case of tryptophan).2. Hydroxyproline, leucine, methionine, phenylalanine, proline, threonine, tryptophan, tyrosine, and valine were found to be resistant and decomposed more slowly than did alanine, arginine, aspartic acid, cystine, glutamic acid, glycine, histidine lysine, and serine. Casein hydrolysate was rapidly and completely deaminated.3. The slow rates of breakdown of the resistant acids when tested singly could not be attributed either to the effects of adsorption on the soil surface or to elimination of an essential Stickland reaction.4. The effect of glucose and of nitrate on anaerobic amino-acid metabolism have been tested. With the exception ofdl-methionine nitrate acted as an hydrogen acceptor in the anaerobic deamination of the resistant acids, glucose had no effect on their anaerobic metabolism.     

Studies on the decomposition of amino acids in soils

Summary 1. The kinetics of decomposition of 17 common amino acids in a garden soil have been followed by percolation techniques that permitted the measurement of O₂-uptake and CO₂-output consequent upon decomposition.2. Most of the amino acids decomposed rapidly; methionine and threonine decomposed much more slowly.3. After decomposition of amino acids in soil, the material residual in the soil had a C : N ratio of about 3 : 1; this possibly represents microbial protein.4. The significance of the results, and the potentialities of the manometric techniques used, are discussed.     

Studies on the decomposition of amino acids in soils

Summary 1. Under soil-percolation conditions the decomposition of amino acids is entirely aerobic.2. Amino-acid decomposition proceeds under aerobic conditions without extra-cellular accumulation of appreciable concentrations of simple soluble organic compounds.3. During leucine decomposition 40 per cent of the leucine-carbon is converted into carbon dioxide while the remaining leucine is synthesised into cellular material. Any carbon dioxide evolved thereafter is due to oxidation of this synthesised cellular material.4. The micro-organisms induced in three different soils in response to leucine percolation had similar abilities in metabolizing different amino acids. The metabolizing abilities of micro-organisms induced in a garden soil in response to percolation withdl-alanine, ordl-aspartic acid, ordl-leucine ordl-phenylalanine have also been studied.5. Progressive drying of soil, stimulated by percolation with specific amino acids, has little effect on its immediate metabolising activity until a low soil-moisture content is reached and the soil particles change colour. At this point the micro-organisms produced by stimulation are irreversibly inactivated.6. The micro-organisms induced in soil/percolate systems in response to leucine percolation are adsorbed by different soils to different extents.     

Effect of exogenous amino acids on the intracellular content of proline and other amino acids in Daucus carota cells

The effect of tryptophan on the biosynthesis of proline has been investigated. Cells of Daucus carota grown in B5 medium supplemented with 5×10^–4M tryptophan acquired the ability to grow in the presence of inhibitory concentrations of azetidine-2-carboxylic acid, an analog of proline. When trp was added to carrot cell cultures at sub-growth inhibiting concentrations, overproduction of intracellular free proline was observed. An increase was also observed for lys, his, ala, leu and phe. Likewise, the addition of asparagine, glutamic acid and phenylalanine to the medium stimulated the intracellular increase of free proline and other amino acids.Abbreviations A2CA azetidine-2-carboxylic acid - 2,4-D 2,4-dichlorophenoxyacetic acid - 5MT 5-methyltryptophan - P5C pyrroline-5-carboxylic acid - f.wt. fresh weight - d.wt. dry weight     

Locations of amino acids in brain slices from the rat. Tetrodotoxin-sensitive release of amino acids

1. Amino acids, particularly glutamate, gamma-aminobutyrate, aspartate and glycine, were released from rat brain slices on incubation with protoveratrine (especially in a Ca(2+)-deficient medium) or with ouabain or in the absence of glucose. Release was partially or wholly suppressed by tetrodotoxin. 2. Tetrodotoxin did not affect the release of glutamine under various incubation conditions, nor did protoveratrine accelerate it. 3. Protoveratrine caused an increased rate of formation of glutamine in incubated brain slices. 4. Increased K(+) in the incubation medium caused release of gamma-aminobutyrate, the process being partly suppressed by tetrodotoxin. 5. Incubation of brain slices in a glucose-free medium led to increased production of aspartate and to diminished tissue contents of glutamates, glutamine and glycine. 6. Use of tetrodotoxin to suppress the release of amino acids from neurons in slices caused by the joint action of protoveratrine and ouabain (the latter being added to diminish reuptake of amino acids), it was shown that the major pools of glutamate, aspartate, glycine, serine and probably gamma-aminobutyrate are in the neurons. 7. The major pool of glutamine lies not in the neurons but in the glia. 8. The tricarboxylic cycle inhibitors, fluoroacetate and malonate, exerted different effects on amino acid contents in, and on amino acid release from, brain slices incubated in the presence of protoveratrine. Fluoroacetate (3mm) diminished the content of glutamine, increased that of glutamate and gamma-aminobutyrate and did not affect respiration. Malonate (2mm) diminished aspartate and gamma-aminobutyrate content, suppressed respiration and did not affect glutamine content. It is suggested that malonate acts mainly on the neurons, and that fluoroacetate acts mainly on the glia, at the concentrations quoted. 9. Glutamine was more effective than glutamate as a precursor of gamma-aminobutyrate. 10. It is suggested that glutamate released from neurons is partly taken up by glia and converted there into glutamine. This is returned to the neurons where it is hydrolysed and converted into glutamate and gamma-aminobutyrate.