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

Human placental chorionic villi were incubated for 30 min with [3H]lysine or [3H]arginine and the distribution ratios (intracellular:extracellular concentrations) were determined. The ratios remained unchanged when Na+ in Earle's buffered salt solution was replaced with Li+. When Na+ was replaced with choline there was a significant increase is distribution ratios (lysine 1.34 +/- 0.33 v. 3.99 +/- 0.15, arginine 1.95 +/- 0.37 v. 5.05 +/- 1.16). Leucine, a neutral amino acid with a Na(+)-independent transport system, was unaffected by choline substitution. The distribution ratio for alanine, which is Na(+)-dependent, was reduced (2.50 +/- 0.41 v. 1.45 +/- 0.20). Two other quarternary amines, acetyl-beta-methylcholine and tetraethylammonium chloride (TEA) caused similar increases in the distribution ratios of the basic amino acids. Hordenine, a tertiary amine, was less effective and there was little or no effect with ephedrine, a secondary amine. The choline effect was first observable at concentrations of 105 mM. With TEA, there was a progressive increase in distribution ratios beginning at 29 mM. Lysine efflux was measured after incubation of villi with lysine in Earle's buffer or choline buffer. Lysine was rapidly released to the fresh medium with 25% more retained in choline-exposed villi. The amines may cause alterations in the kinetics of basic amino-acid transporters or may modify other aspects of placental physiology permitting an increase retention of the basic amino acids.

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Basic amino acid transport in renal papilla: microinfusion of Henle's loops and vasa recta

AJP Renal Physiology ◽

10.1152/ajprenal.1993.265.6.f830 ◽

1993 ◽

Vol 265 (6) ◽

pp. F830-F838 ◽

Cited By ~ 4

Author(s):

W. H. Dantzler ◽

S. Silbernagl

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Transport ◽

Basic Amino Acid ◽

Renal Papilla ◽

Tubular Structures ◽

Acid Transport ◽

Basic Amino Acids ◽

Neutral Amino Acids ◽

Vasa Recta

To determine whether basic amino acids, like acidic and neutral amino acids, could be reabsorbed distal to tips of Henle's loops and recycled between loops and vasa recta in the renal papilla, we continuously microinfused ascending Henle's loops and vasa recta with 14C-labeled L-lysine (L-Lys; 1.28 mM) or L-arginine (L-Arg; 1.17 mM) and 3H-labeled inulin. We also determined percent of recovered radiolabel as intact amino acid. Like acidic and neutral amino acids, relative to inulin, approximately 30% of L-Lys and approximately 45% of L-Arg microinfused into Henle's loops were reabsorbed. However, whereas radiolabeled L-Lys reabsorption, like reabsorption of acidic and neutral amino acids, was not readily inhibited, radiolabeled L-Arg reabsorption was reduced to approximately 25% by addition of unlabled L-Arg (50 mM) or L-homoarginine (L-Homo-Arg) (50 mM) to infusate. This observation provides greater evidence for specific, carrier-mediated reabsorption for L-Arg than for acidic or neutral amino acids. About 36% (relative to inulin) of each of these amino acids microinfused into ascending vasa recta apparently was transferred directly into ipsilateral tubular structures (probably thin descending limbs of Henle's loops). Transfer of radiolabeled L-Arg was reduced to approximately 8% by the inclusion of unlabeled L-Arg (50 mM) in infusate. Transfer of unlabeled L-Lys was unaffected by inclusion of unlabeled L-Lys (50 mM) in infusate but was reduced to approximately 20% by inclusion of unlabeled L-Arg (50 mM) or L-Homo-Arg (50 mM) in infusate. (ABSTRACT TRUNCATED AT 250 WORDS)

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High sensitivity of Xenopus gustatory receptors to amino acids and bitter substances

AJP Regulatory Integrative and Comparative Physiology ◽

10.1152/ajpregu.1982.243.1.r42 ◽

1982 ◽

Vol 243 (1) ◽

pp. R42-R48 ◽

Cited By ~ 3

Author(s):

K. Yoshii ◽

C. Yoshii ◽

Y. Kobatake ◽

K. Kurihara

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Xenopus Laevis ◽

High Sensitivity ◽

Basic Amino Acid ◽

Gustatory Receptors ◽

Basic Amino Acids ◽

Neutral Amino Acids ◽

Gustatory Nerve ◽

Cross Adaptation

The gustatory nerve responses of the aquatic toad Xenopus laevis to salts, acids, amino acids, and bitter substances were recorded. 1) The gustatory receptors were sensitive to amino acids and bitter substances. The thresholds were 10(-7) M for Arg, 3 X 10(-9) M for strychnine, and 3 X 10(-8) M for quinine, 200-20,000 times lower than the thresholds for the respective stimuli in the bullfrog. 2) The basic and the neutral amino acids were effective whereas the acidic ones were not. Relations between the responses and log stimulus concentrations for the basic amino acids were linear in a wide concentration range whereas those for the neutral ones were of S shape. Cross-adaptation did not occur among pairs of a basic amino acid and a neutral one. 3) Responses to the basic amino acids and the basic bitter substances were suppressed by the addition of salts to the stimulating solutions, while those to the neutral and the acidic substances were not suppressed.

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Basic Amino Acids as Intracellular Cations in K Deficiency

American Journal of Physiology-Legacy Content ◽

10.1152/ajplegacy.1958.193.3.644 ◽

1958 ◽

Vol 193 (3) ◽

pp. 644-652 ◽

Cited By ~ 26

Author(s):

Robert E. Eckel ◽

James E. C. Norris ◽

Charles E. Pope

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Acid Content ◽

Amino Acid Content ◽

Basic Amino Acid ◽

Basic Amino Acids ◽

Microbiological Techniques ◽

K Deficiency ◽

Desoxycorticosterone Acetate

Rats were made K deficient by diet, by the injection of desoxycorticosterone acetate, and by protein repletion of protein depleted rats fed K-free diets. The tissues were examined for increases in basic amino acids. Increased amounts of l (+) lysine, identified by chromatographic, electrophoretic, enzymatic and microbiological techniques have been found in the muscle and kidney of K-deficient animals. The lysine and/or the basic amino acid content as well as the Na, K and Cl content of muscle and plasma has been measured. Lysine contributes significantly to the total cations of muscle in K deficiency. On partial K repletion, some of this lysine is apparently completely oxidized.

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Faculty Opinions recommendation of Deorphanization of GPRC6A: a promiscuous L-alpha-amino acid receptor with preference for basic amino acids.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1024356.287883 ◽

2005 ◽

Author(s):

Joseph Heitman

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Acid Receptor ◽

Basic Amino Acids ◽

Alpha Amino Acid

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Determination of Methylated Basic Amino Acids with the Amino Acid Analyzer

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)44121-5 ◽

1973 ◽

Vol 248 (7) ◽

pp. 2387-2391 ◽

Cited By ~ 1

Author(s):

Gladys E. Deibler ◽

Russell E. Martenson

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Basic Amino Acids ◽

Amino Acid Analyzer

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

Journal of Bacteriology ◽

10.1128/jb.181.17.5426-5432.1999 ◽

1999 ◽

Vol 181 (17) ◽

pp. 5426-5432 ◽

Cited By ~ 38

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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Amino acid recognition by fine tuning the association constants: tailored naphthalimides in pillar[5]arene-based indicator displacement assays

RSC Advances ◽

10.1039/c6ra15003a ◽

2016 ◽

Vol 6 (89) ◽

pp. 86269-86275 ◽

Cited By ~ 23

Author(s):

Márton Bojtár ◽

Adrien Paudics ◽

Dóra Hessz ◽

Miklós Kubinyi ◽

István Bitter

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Association Constants ◽

Fine Tuning ◽

Supramolecular Interactions ◽

Basic Amino Acids ◽

Anchoring Groups ◽

Displacement Assays ◽

Amino Acid Recognition

Three naphthalimide derivatives were synthesized with different anchoring groups to adjust the supramolecular interactions with carboxylato-pillar[5]arene. The complexes were used as indicator displacement assays for basic amino acids and diamines.

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Photochromic and photothermal hydrogel derived from natural amino acid and heteropoly acid

Soft Matter ◽

10.1039/d1sm01272j ◽

2021 ◽

Author(s):

Xue Wang ◽

Xiaohuan Liu ◽

Zhiyuan Ma ◽

Chuanling Mu ◽

Wen Li

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Heteropoly Acid ◽

Acidic Condition ◽

Heteropoly Acids ◽

Natural Amino Acid ◽

Basic Amino Acids

A new kind of supramolecular hydrogels have been designed and synthesized via the co-assembly of basic amino acids (AAs) and heteropoly acids (HPAs) under acidic condition. The formation of gel-like...

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Self-healing hydrogels triggered by amino acids

Organic Chemistry Frontiers ◽

10.1039/c6qo00476h ◽

2016 ◽

Vol 3 (12) ◽

pp. 1699-1704 ◽

Cited By ~ 10

Author(s):

Nicola Zanna ◽

Andrea Merlettini ◽

Claudia Tomasini

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Aspartic Acid ◽

Chemical Properties ◽

Aromatic Amino Acids ◽

Self Healing ◽

Acidic Amino Acid ◽

Basic Amino Acids

Nine amino acids with different chemical properties have been chosen to promote the formation of hydrogels based on the bolamphiphilic gelator A: three basic amino acids (arginine, histidine and lysine), one acidic amino acid (aspartic acid), two neutral aliphatic amino acids (alanine and serine) and three neutral aromatic amino acids (phenylalanine, tyrosine and tryptophan).

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