Arginine test

The biuret reaction [alkaline Cu(II)] and the arginine test [102] are used to detect peptides in nucleic acid preparations. Two other colour reactions permit either type of nucleic acid to be detected in the presence of the other one is due to Dische and the other is the phloroglucinol test of v. Etjler and Hahn. 

A variety of L-arginine-based inhibitors was tested by Komori and coworkers114. They found AG-methoxy-L-arginine as well as AG-hydroxy-L-arginine and L-arginine itself to oxidize NADPH. The mechanism of the effects remain to be determined. 

Cole test (1901) for tryptophan, and the Sakaguchi reaction for arginine (1925). 

The methods used were acrosin proteolytic activity (APA) assay (with gelatin) and acrosin activity assay with N-a-benzoyl-DL-arginine-p-nitroanihde (BAPNA)-Triton X 100, and BAPNA assay for trypsin activity [9-11]. The antioxidant activity was tested spectrometrical with ABTS+ [12]. Cytotoxicity of extracts was determined by MTT Cell Proliferation Assay [13]. 

Bacillus subtilis transformants were identified by their resistance to naphthalene, parachlorobiphenyl, or dibenzofuran. Controls subtilis protoplasts regenerated without the addition of B. megaterium plasmid DNA) exhibited no increased reistance to these three compounds. That each transformant was B. subtilis and not a contaminant was verified by testing for the B. subtilis chromosomal markers. Only streptomycin resistant strains that showed arginine and leucine dependent growth were used in subsequent experiments. 

Biochemistry and chemistry takes place mostly in solution or in the presence of large quantities of solvent, as in enzymes. As the necessary super-computing becomes available, molecular dynamics must surely be the method of choice for modeling structure and for interpreting biological interactions. Several attempts have been made to test the capability of molecular dynamics to predict the known water structure in crystalline hydrates. In one of these, three amino acid hydrates were used serine monohydrate, arginine dihydrate and homoproline monohydrate. The first two analyses were by neutron diffraction, and in the latter X-ray analysis was chosen because there were four molecules and four waters in the asymmetric unit. The results were partially successful, but the final comments of the authors were "this may imply that methods used currently to extract potential function parameters are insufficient to allow us to handle the molecular-level subtleties that are found in aqueous solutions" (39). 

Turtles also use chemical cues for food, as shown for the marine loggerhead turtle, Caretta caretta (Grassman etal., 1984). Among freshwater turtles, the European pond turtle, Emys orbicularis, locates food hy chemoreception. This species moves chemical stimuli from the pond water to the chemoreceptors of the nasal and oral cavities by slow jaw testing movements . The frequency of these movements increases in response to the amino acids alanine, arginine. 

Catalytic tests were performed in a glass vessel equipped with a stirrer motor. Two monoliths (diameter 4.3 cm, length 4 cm) were mounted in plane on the stirrer axis. The total reaction volume was 2.5 1. Lipase was assayed in the acylation of vinyl acetate with butanol in toluene. Initial reaction rate was followed by GC analysis. Immobilized trypsin was used in the hydrolysis of N-benzoyl-l-arginine ethyl ester (BAEE) in a 0.01 M phosphate buffer pH 8 at 308 K. The reaction was followed by UV-VIS at 253 nm, and reaction rate was calculated in the mass transfer limited situation. 

Total protein, albumin, urea (standard methods) and middle molecules (MM) were determined in citrated plasma [6]. The trypsin-like activity (TLA) of plasma was measured using the chromogenic peptide substrate (Z-glycyl-glycyl-L-arginine-4-nitroanilide) [7]. Evaluation of anti-enzymatic potential in plasma was based on concentrations of the main protease inhibitors -proteinase inhibitor (ttj-PI) and aj-macroglobulin (a -M). Student s t-test was used for statistical analysis. 

The previously described test system involving in vitro analysis of fat body vitellogenin production and secretion is apparently distinctive in providing evidence for canavanine-mediated curtailment of protein synthesis. At least, canavanine attenuates the amount of [ Hjleucine-labeled protein secreted by the fat body (Fig. 1). As shown in figure 1, the effect of arginine depletion itself is debilitating and it becomes increasingly deleterious with time—quite apart from any effect canavanine may elicit. With increased treatment time, canavanine-... 

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