Accumulation, selection and covariation of amino acids in sieve tube sap of tansy (Tanacetum vulgare) and castor bean (Ricinus communis): evidence for the function of a basic amino acid transporter and the absence of a γ-amino butyric acid transporter

2014 ◽  
Vol 152 (1) ◽  
pp. 130-137
Author(s):  
Susanne N. Bauer ◽  
Heike Nowak ◽  
Frank Keller ◽  
Jose Kallarackal ◽  
Mohamad-Reza Hajirezaei ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Butyric Acid ◽  
Castor Bean ◽  
Ricinus Communis ◽  
Sieve Tube ◽  
Basic Amino Acid ◽  
Tanacetum Vulgare ◽  
Amino Butyric Acid ◽  
Acid Transporter

Changes in amino acid compounds of wheat plants during ensiling and aerobic exposure: the influence of propionic acid and urea phosphate-calcium propionate

1984 ◽  
Vol 102 (3) ◽  
pp. 667-672 ◽  
Author(s):  
G. Ashbell ◽  
H. H. Theune ◽  
D. Sklan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Propionic Acid ◽  
Butyric Acid ◽  
Total Amino Acid ◽  
Amino Butyric Acid ◽  
Urea Phosphate ◽  
Fresh Material ◽  
Calcium Propionate

SummaryChanges in distribution of amino acid nitrogen of chopped wheat plants ensiled at shooting and flowering when wilted, and at the milk and dough stages as fresh material, were determined as affected by addition of 0·8% propionic acid (PrA) or 2·2% urea phosphate-calcium propionate (UP-CaPr). Analyses were carried out after an ensiling period of 90 days and after a further aerobic exposure period (AE) of 7 days.Total amino acid (TAA) contents in the dry matter (D.M.) during the fermentation period and in the AE were stable in untreated material (UM) and treated material. Concentration of essential amino acids decreased during fermentation, this decrease being higher in the UM. The free amino acids were low in the fresh material (18·6% of TAA) but increased in the ensiled material to ca. 71 % of the TAA in the silage. In the AE this level was 63% in UM and 69% in treated material. The ammonia-N contents increased during fermentation in UM and especially in the UP-CaPr treatments, while the opposite occurred in the PrA treatments.The concentrations of and changes in 21 amino acids (AAs) are given. The highest AA concentrations recorded in the fresh material were those of arginine, lysine, glutamic acid, alanine, leucine, proline and glycine. The most marked increments in AAs as a result of fermentation were those of ornithine, γ-amino butyric acid, threonine and methionine. Marked decreases were observed in glutamine, arginine and glutamic acid. PrA increased mainly arginine, asparagine and glutamine, whereas γ-amino butyric acid decreased; UP-CaPr increased arginine, asparagine, lysine and glutamic acid (in silage only) and reduced γ-amino butyric acid and glutamine (in AE only).

The free amino-acids present in fresh and in fermented marrow stem kale

1954 ◽  
Vol 45 (1) ◽  
pp. 36-40 ◽  
Author(s):  
Hamish Robertson ◽  
A. John G. Barnett
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Butyric Acid ◽  
Sulphur Dioxide ◽  
Free Amino Acids ◽  
Free Amino ◽  
Amino Acid Pattern ◽  
Amino Butyric Acid ◽  
Partial Sterilization

1. An investigation has been made into the changes that take place in the free amino-acid pattern when kale-water slurries are allowed to ferment under conditions of (a) aeration, (b) anaerobiasis and (c) partial sterilization with sulphur dioxide.2. It has been found that, with aerated mixtures, the loss of free amino-acids is virtually complete within 2 weeks, while there is only a slight loss with the anaerobic mixtures. With mixtures containing sulphur dioxide no loss of amino-acids occur.3. The formation of α-amino butyric acid possibly from threonine has been noted.

AMINO ACID ANALYSES OF THE SPECIES IN THE GENUS GOSSYPIUM

1968 ◽  
Vol 10 (2) ◽  
pp. 362-368 ◽  
Author(s):  
Patricia Sarvella ◽  
B. J. Stojanovic
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Butyric Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Protein Amino Acid ◽  
Amino Butyric Acid ◽  
Dna Base ◽  
Protein Amino Acids

The free and protein amino acid patterns present in the leaves of the species of the genus Gossy pium were determined. The presence or absence of the free amino acids except for glycine and γ-amino butyric acid did not appear to be of value for separation of the species. However, the patterns of the protein amino acids varied between the genomes, and seemed to separate the species. These patterns were separated into groups similar to those found for the DNA-base ratios and the cytotaxonomic grouping of the species.

THE UTILIZATION OFD-AMINO ACIDS BY YEASTS

1967 ◽  
Vol 13 (7) ◽  
pp. 777-788 ◽  
Author(s):  
T. A. LaRue ◽  
J. F. T. Spencer
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nitrogen Source ◽  
Butyric Acid ◽  
Amino Butyric Acid

Ninety-one strains of yeast from 19 genera were examined for their ability to utilize single L- and D-amino acids as the nitrogen source for growth. Eighty strains from 17 genera were able to grow on at least one D-amino acid. The most readily utilized were alanine, α-amino butyric acid, leucine, and serine. D-Cysteine was used by few species. The utilization of D-amino acids is of little use in classifying or identifying yeasts.

scholarly journals Neutral amino acid transporter ASCT2 displays substrate-induced Na+ exchange and a substrate-gated anion conductance

2000 ◽  
Vol 346 (3) ◽  
pp. 705-710 ◽  
Author(s):  
Angelika BRÖER ◽  
Carsten WAGNER ◽  
Florian LANG ◽  
Stefan BRÖER
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Anion Channel ◽  
Amino Acid Transporter ◽  
Neutral Amino Acid ◽  
Xenopus Laevis Oocytes ◽  
Anion Conductance ◽  
Neutral Amino Acid Transporter ◽  
Inward Currents ◽  
Acid Transporter

The neutral amino acid transporter ASCT2 mediates electroneutral obligatory antiport but at the same time requires Na+ for its function. To elucidate the mechanism, ASCT2 was expressed in Xenopus laevis oocytes and transport was analysed by flux studies and two-electrode voltage clamp recordings. Flux studies with 22NaCl indicated that the uptake of one molecule of glutamine or alanine is accompanied by the uptake of four to seven Na+ ions. Similarly to the transport of amino acids, the Na+ uptake was mediated by an obligatory Na+ exchange mechanism that depended on the presence of amino acids but was not stoichiometrically coupled to the amino acid transport. Other cations could not replace Na+ in this transport mechanism. When NaCl was replaced by NaSCN in the transport buffer, the superfusion of oocytes with amino acid substrates resulted in large inward currents, indicating the presence of a substrate-gated anion channel in the ASCT2 transporter. The Km for glutamine derived from these experiments is in good agreement with the Km derived from flux studies; it varied between 40 and 90 μM at holding potentials of -60 and -20 mV respectively. The permeability of the substrate-gated anion conductance decreased in the order SCN- NO3- > I- > Cl- and also required the presence of Na+.

Basic amino acid induced isomerization of a spiropyran: towards visual recognition of basic amino acids in water

2007 ◽  
Vol 31 (11) ◽  
pp. 1878 ◽  
Author(s):  
Yuanyuan Liu ◽  
Meigong Fan ◽  
Shuxiao Zhang ◽  
Xiaohai Sheng ◽  
Jiannian Yao
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Visual Recognition ◽  
Basic Amino Acid ◽  
Basic Amino Acids

scholarly journals Multiple components of arginine and phenylalanine transport induced in neutral and basic amino acid transporter-cRNA-injected Xenopus oocytes

1996 ◽  
Vol 318 (3) ◽  
pp. 915-922 ◽  
Author(s):  
George J PETER ◽  
Iain G. DAVIDSON ◽  
Aamir AHMED ◽  
Lynn McILROY ◽  
Alexander R. FORRESTER ◽  
...  
Keyword(s):  
Amino Acid ◽  
Xenopus Oocytes ◽  
Competitive Inhibition ◽  
Protein Complexes ◽  
Basic Amino Acid ◽  
Amino Acid Transporter ◽  
Transport Processes ◽  
Arginine Transport ◽  
Acid Transporter ◽  
Phenylalanine Transport

The induced uptakes of l-[3H]phenylalanine and l-[3H]arginine in oocytes injected with clonal NBAT (neutral and basic amino acid transporter) cRNA show differential inactivation by pre-treatment with N-ethylmaleimide (NEM), revealing at least two distinct transport processes. NEM-resistant arginine transport is inhibited by leucine and phenylalanine but not by alanine or valine; mutual competitive inhibition of NEM-resistant uptake of arginine and phenylalanine indicates that the two amino acids share a single transporter. NEM-senstive arginine transport is inhibited by leucine, phenylalanine, alanine and valine. At least two NEM-sensitive transporters may be expressed because we have been unable to confirm mutual competitive inhibition between arginine and phenylalanine transport. The NEM-resistant transport mechanism appears to involve distinct but overlapping binding sites for cationic and zwitterionic substrates. NBAT is known to form oligomeric protein complexes in cell membranes, and its functional roles when expressed in Xenopus oocytes may include interaction with oocyte proteins, leading to increased native amino acid transport activities; these resemble NBAT-expressed activities in terms of NEM-sensitivity and apparent substrate range (including an unusual inhibition by β-phenylalanine).

scholarly journals Amino Acid-Mediated Induction of the Basic Amino Acid-Specific Outer Membrane Porin OprD from Pseudomonas aeruginosa

1999 ◽  
Vol 181 (17) ◽  
pp. 5426-5432 ◽  
Author(s):  
Martina M. Ochs ◽  
Chung-Dar Lu ◽  
Robert E. W. Hancock ◽  
Ahmed T. Abdelal
Keyword(s):  
Amino Acids ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Regulatory Protein ◽  
Basic Amino Acid ◽  
Sole Source ◽  
Activation Mechanism ◽  
Beta Lactam ◽  
Mobility Shift ◽  
Carbon And Nitrogen

ABSTRACT Pseudomonas aeruginosa can utilize arginine and other amino acids as both carbon and nitrogen sources. Earlier studies have shown that the specific porin OprD facilitates the diffusion of basic amino acids as well as the structurally analogous beta-lactam antibiotic imipenem. The studies reported here showed that the expression of OprD was strongly induced when arginine, histidine, glutamate, or alanine served as the sole source of carbon. The addition of succinate exerted a negative effect on induction ofoprD, likely due to catabolite repression. The arginine-mediated induction was dependent on the regulatory protein ArgR, and binding of purified ArgR to its operator upstream of theoprD gene was demonstrated by gel mobility shift and DNase assays. The expression of OprD induced by glutamate as the carbon source, however, was independent of ArgR, indicating the presence of more than a single activation mechanism. In addition, it was observed that the levels of OprD responded strongly to glutamate and alanine as the sole sources of nitrogen. Thus, that the expression ofoprD is linked to both carbon and nitrogen metabolism ofPseudomonas aeruginosa.

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