Tissue Amino Acids In Rats Fed Norleucine, Norvaline, Homoarginine or Other Amino Acid Analogues

The cumulative entry of amino acids into Ehrlich ascites carcinoma cells is due to the presence of active transport systems, each with its own specific range of substrates. Several amino acids and amino acid analogues may have an affinity for the same transport system and thus may inhibit transport of other amino acids by acting as competitive inhibitors or competitive substrates. Loss of methionine from ascites cells takes place by a diffusion process which obeys Fick's law. Leucine accumulation by ascites cells is small and is increased on addition of certain other amino acids. The increase is not due to inhibition of leucine oxidation as increase in the rate of production of radioactive carbon dioxide from labeled leucine also occurs. Kinetic aspects of these results are discussed.

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Effect of a Leucine Analogue on Incorporation of Glycine into the Proteins of Explanted Chick Embryos

Development ◽

10.1242/dev.6.2.262 ◽

1958 ◽

Vol 6 (2) ◽

pp. 262-269

Author(s):

Phyllis W. Schultz ◽

Heinz Herrmann

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Chick Embryo ◽

Total Protein ◽

Nutrient Medium ◽

Chick Embryos ◽

Agar Gel ◽

Egg Extract ◽

Amino Acid Analogues

Amino acid analogues have been observed to give rise to abnormal forms of development of chick and amphibian embryos (Herrmann, 1953; Rothfels, 1954; Waddington & Sirlin, 1954; Feldman & Waddington, 1955; Herrmann, Rothfels-Konigsberg, & Curry, 1955). Assuming that these disturbances may be due to interference with the utilization of amino acids for protein formation, we have attempted an analysis of this effect by comparison of the protein contents and of the uptake of glycine into the proteins of chick embryo explants in the presence and absence of amino acid analogues. The results of such experiments are reported in this paper. The chick embryos used for explanation, the explantation technique, and the determination of total protein glycine and of tracer glycine were essentially the same as described previously (Herrmann & Schultz, 1958). The embryos were explanted at the 11–13 somite stage on to the surface of an agar gel containing egg extract as nutrient medium following the procedure given by Spratt (1947) as modified by Rothfels (1954).

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Chelating polymers. I. The synthesis and acid dissociation behavior of several N-(p-vinylbenzenesulfonyl)-substituted diaminopolyacetic acid monomers, monomeric analogues, and related intermediates

Canadian Journal of Chemistry ◽

10.1139/v70-023 ◽

1970 ◽

Vol 48 (1) ◽

pp. 163-175 ◽

Cited By ~ 13

Author(s):

R. M. Genik-Sas-Berezowsky ◽

I. H. Spinner

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Dissociation Constants ◽

Acid Dissociation ◽

Inductive Effects ◽

Cyclic Amide ◽

Amino Acid Analogues ◽

Related Compounds ◽

Chelating Polymers ◽

Made In

Two new chelating monomers, N-(p-vinylbenzenesulfonyl)1,2-diaminoethane-N′,N′-diacetic (SS-EDDA) and -N,N′,N′-triacetic (SS-ED3A) acids, as well as several monomeric analogues and related intermediates have been prepared. In addition, 2-oxo-1-piperazine acetic (S-KP), 3-oxo-1-piperazine acetic (U-KP), and 2-oxo-1,4-piperazine diacetic (3-KP) acids have been synthesized and the interconvertibility between these cyclic amides and their unsubstituted linear amino acid analogues, ethylene-diamine-N,N′-diacetic (S-EDDA), -N,N-diacetic (U-EDDA), and -N,N,N′-triacetic (ED3A) acids respectively, was demonstrated.The acid dissociation constants of the various amino acids were determined potentiometrically at 25° and μ = 0.1 M(KNO3) and the results were compared with the hydrogen ion affinities of related compounds. Dissociation schemes were proposed for all the compounds based on these results. Rationalizations of the linear amino acid and the cyclic amide dissociation constants were made in terms of the effects of cyclization and the inductive effects of neighboring groups. These rationalizations were found to be helpful in clarifying the dissociation schemes previously proposed for several of the linear amino acids.

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Food Intake, Growth and Tissue Amino Acids in Rats Fed Amino Acid Analogues

Journal of Nutrition ◽

10.1093/jn/115.9.1180 ◽

1985 ◽

Vol 115 (9) ◽

pp. 1180-1195 ◽

Cited By ~ 7

Author(s):

Jean K. Tews ◽

Alfred E. Harper

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Food Intake ◽

Amino Acid Analogues

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KINETICS OF AMINO ACID INCORPORATION INTO SERUM PROTEINS

The Journal of General Physiology ◽

10.1085/jgp.38.3.283 ◽

1955 ◽

Vol 38 (3) ◽

pp. 283-293 ◽

Cited By ~ 37

Author(s):

H. Green ◽

H. S. Anker

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Serum Protein ◽

Transit Time ◽

Serum Proteins ◽

Amino Acid Incorporation ◽

Acid Incorporation ◽

Amino Acid Analogues ◽

Kinetics Of

1. The effect of varying body temperature on the rate of amino acid incorporation into serum protein does not give support to the idea that the rate of this process is adjusted in vivo to restore those protein molecules destroyed by thermal denaturation. The experimentally observed Q10 was about 3.9. 2. When amino acids are injected into the blood of animals in a steady state of serum protein turnover, a period of time elapses before these amino acids can be found in the serum proteins. This has been called transit time. At a given temperature (31°) it is the same in rabbits, turtles, and Limulus (1 hour). In rabbits and turtles it has a Q10 of 3.2. It appears to be specifically related to the process of synthesis (or release) of serum proteins. 3. It was not possible to affect the transit time or the incorporation rate by the administration of amino acid analogues.

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AMINO ACIDS AS CENTRAL NERVOUS TRANSMITTERS: THE INFLUENCE OF IONS, AMINO ACID ANALOGUES, AND ONTOGENY ON TRANSPORT SYSTEMS for l-GLUTAMIC AND l-ASPARTIC ACIDS AND GLYCINE INTO CENTRAL NERVOUS SYNAPTOSOMES OF THE RAT

Journal of Neurochemistry ◽

10.1111/j.1471-4159.1973.tb06037.x ◽

1973 ◽

Vol 21 (6) ◽

pp. 1533-1550 ◽

Cited By ~ 227

Author(s):

J. P. Bennett ◽

W. J. Logan ◽

S. H. Snyder

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Transport Systems ◽

Amino Acid Analogues

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Amino acids induce renal vasodilatation in isolated perfused kidney: coupling to oxidative metabolism

AJP Heart and Circulatory Physiology ◽

10.1152/ajpheart.1984.247.6.h999 ◽

1984 ◽

Vol 247 (6) ◽

pp. H999-H1004 ◽

Cited By ~ 4

Author(s):

M. Brezis ◽

P. Silva ◽

F. H. Epstein

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Rat Kidney ◽

O2 Consumption ◽

Metabolic Substrates ◽

Parallel Increase ◽

Protein Feeding ◽

Amino Acid Analogues ◽

Renal Vascular ◽

Dose Dependent

Renal vasodilatation regularly accompanies protein feeding and amino acid infusions, but the mechanism is unknown. The effects of several different amino acids on renal hemodynamics were studied in the isolated rat kidney, perfused with glucose as the only other substrate. Addition of amino acids produced a dose-dependent, brisk, and sustained decrease in renal vascular resistance (by 5–35%) without change in glomerular filtration rate (GFR). The vasodilatation was associated with a parallel increase in O2 consumption (increases QO2). The effect was most marked with amino acids actively metabolized by the kidney, such as glutamine (at 2 mM), but was seen with most amino acids at 8 mM. The amino acid analogues alpha-aminobutyrate, taurine, and cycloleucine, cotransported with sodium but not metabolized, did not cause significant vasodilatation or increases QO2. Blocking active transport with ouabain blunted the amino acid-induced vasodilatation and increases QO2. Similar resistance to amino acids was produced by halting GFR with hyperoncotic medium. Restoration of GFR by increasing perfusion pressure in the presence of hyperoncotic medium reestablished amino acid-induced vasodilatation and increases QO2. Furosemide did not block the vasodilatory response. Inhibition of mitochondrial respiration by antimycin blocked both vasodilatation and increases QO2, but rotenone blockade could be bypassed by succinate or glutamine. Amino acids have a direct vasodilating action on isolated kidneys probably related to their role as metabolic substrates and linked to an increase in renal O2 consumption.

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INHIBITION OF RUST DEVELOPMENT ON DETACHED WHEAT LEAVES BY METABOLITES, ANTIMETABOLITES, AND ENZYME POISONS

Canadian Journal of Botany ◽

10.1139/b60-043 ◽

1960 ◽

Vol 38 (4) ◽

pp. 467-476 ◽

Cited By ~ 29

Author(s):

D. J. Samborski ◽

F. R. Forsyth

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Sodium Fluoride ◽

Sodium Azide ◽

Sugar Alcohols ◽

Detached Leaves ◽

Amino Acid Analogues ◽

Wheat Leaves ◽

Natural Amino Acids ◽

Purines And Pyrimidines

The effect of metabolites and antimetabolites on rust development was studied, using detached leaves of Little Club wheat floated on solutions containing benzimidazole plus the compound under study. Purines and pyrimidines, vitamins, amino acids, carbohydrates, and enzyme poisons were tested. A number of these compounds inhibited leaf and stem rusts of wheat at concentrations that were not injurious to the host. Of the purines and pyrimidines that were tested, thymine and the analogue azathymine were the only effective inhibitors. The antivitamin oxythiamine was inhibitory and the inhibition was competitively reversed by thiamine.A few natural amino acids, notably histidine, isoleucine, methionine, and serine, inhibited rust development. The inhibition was reversed by glycine in all cases except with serine. Amino acid analogues, particularly canavanine, ethionine, and p-fluorophenylalanine, were excellent inhibitors; the inhibitions were reversed by comparable levels of arginine, methionine, and phenylalanine respectively. The carbohydrates lyxose, xylose, sorbose, and all the sugar alcohols tested were effective inhibitors of rust development. Of the enzyme poisons tested, sodium fluoride and sodium azide differentially inhibited rust growth.

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