Veränderungen der Hämolymphe vor der Verpuppung von Cerura vinula L.: Der Gehalt an Eiweiß, Aminosäuren, Ommochrom-Vorstufen und Ommochromen

1966 ◽  
Vol 21 (12) ◽  
pp. 1184-1195 ◽  
Author(s):  
Detlef Bückmann ◽  
Axel Willig ◽  
Bernt Linzen
Keyword(s):  
Amino Acids ◽  
Ion Exchange ◽  
Free Amino ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Total Carbohydrate ◽  
Protein Nitrogen ◽  
Metabolic Alterations ◽  
Total Free Amino Acids ◽  
Free Aminoacids

Ommochrome synthesis at the beginning of lepidopteran metamorphosis is correlated to morpholytic and morphogenetic activity. In order to examine the metabolic alterations involved, data on respiration, haemolymph volume and on concentrations of total carbohydrate, soluble protein and non-protein nitrogen have been collected. Free aminoacids were separated by ion exchange chromatography and the levels of tryptophan, 3-hydroxy-kynurenine and of total ommochromes were determined independently at different stages during transformation of the larva towards the pupa. While the levels of non-protein nitrogen and of total free amino acids remain nearly constant, there is a three- and twentyfold increase of tryptophan and 3-hydroxy-kynurenine, respectively. It is proposed, that ommochrome formation serves in the removal of tryptophan liberated by proteolysis.

AMINO ACID COMPOSITION OF UREDOSPORES OF PUCCINIA GRAMINIS TRITICI

1965 ◽  
Vol 43 (6) ◽  
pp. 695-699 ◽  
Author(s):  
David Stefanye ◽  
Kenneth R. Bromfield
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Ion Exchange ◽  
Free Amino Acids ◽  
Free Amino ◽  
Spore Wall ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Puccinia Graminis ◽  
Total Free Amino Acids

Uredospores of Puccinia graminis var. tritici (race 56) were analyzed quantitatively for total free amino acids and ninhydrin-positive substances by ion-exchange chromatography. Extracts of these substances were obtained by leaching the spores and by re-extracting leached spores with boiling water. Thirty-five ninhydrin-positive compounds were found and identified. The leach extract differed quantitatively from the extract obtained by boiling although both contained the same 35 substances. It is proposed that there are easily extractable ninhydrin-positive substances coating the spore wall and ninhydrin-positive substances in the protoplasm that can be extracted only with difficulty.

scholarly journals Free amino acids in fruit bodies of some wood destroying fungi

2014 ◽  
Vol 14 (1-2) ◽  
pp. 151-155
Author(s):  
Wiesław Tadeusiak ◽  
Eliza Balicka
Keyword(s):  
Amino Acids ◽  
Ion Exchange ◽  
Free Amino Acids ◽  
Free Amino ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Polyporus Squamosus

Concentration of free amino acids in the following bracket fungi: <i>Climacodon septentrionalis</i> (Fr) P. Karst, <i>Hapalopilus croceus</i> (Pers. ex Fr.) Donk., <i>Laetiporusus sulphurens</i> (Bull. ex Fr.) Murill and <i>Polyporus squamosus</i> Huds ex Fr., were determined by ion-exchange chromatography.

Effect of Deproteinating Agents (Picric Acid and Sulfosalicylic Acid) on Analysis for Free Amino Acids in Swine Blood and Tissue

1969 ◽  
Vol 52 (5) ◽  
pp. 981-984 ◽  
Author(s):  
J E Knipfel ◽  
D A Christensen ◽  
B D Owen
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Ion Exchange ◽  
Free Amino ◽  
Biological Fluids ◽  
Picric Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Sulfosalicylic Acid ◽  
Coefficients Of Variation

Abstract Amino acid analyses were performed on samples of blood, liver tissue, loin muscle, and ham muscle by ion exchange chromatography after deproteination of the samples with picric acid or sulfosalicylic acid (SSA). Resolution of threonine and serine from the ion exchange column was poor when SSA was used as the deproteinating agent. Twelve of sixteen amino acids were higher (P &lt; 0.05) in serum deproteinated with picric acid as compared to concentrations determined after SSA deproteination. Amino acid values for ham muscle tended to be higher after deproteination with picric acid; however, with liver and loin muscle samples, the values were somewhat higher after SSA deproteination. In both serum and tissue analyses, coefficients of variation were lower for niGSt amino acids when picric acid was utilized as the deproteinating agent. The latter observation, in particular, suggests that picric acid is preferable to SSA as a deproteinating agent before amino acid analyses of biological fluids. Standardization of methods of deproteination is needed to allow meaningful comparisons of data.

The non-protein nitrogen composition of grass silages: I. The estimation of the basic amino acids and non-volatile amines by chromatography on a weak cation exchange resin

1969 ◽  
Vol 72 (3) ◽  
pp. 459-466 ◽  
Author(s):  
A. D. Hughes
Keyword(s):  
Amino Acids ◽  
Ion Exchange ◽  
Cation Exchange ◽  
Exchange Resin ◽  
Cation Exchange Resin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Protein Nitrogen ◽  
Weak Cation Exchange

SUMMARYInvestigations into the non-protein nitrogen composition of grass silages using the 50 cm strong cation-exchange column of Spackman, Stein & Moore (1958) to determine the basic amino acids led to difficulties in the determination of ethanolamine in the presence of high concentrations of ammonia, and of histidine in the presence of δ amino-n-valeric acid. An alternative technique for the ion exchange chromatography and estimation of histidine, lysine, ornithine, ethanolamine, arginine and ammonia on a weak cation-exchange resin has been developed. This method enables small amounts of ethanolamine to be determined in the presence of large amounts of ammonia and values for the ethanolamine content of a number of silage samples are presented. When used in conjunction with the technique of Spackman et al. (1958) the δ-amino-n-valeric acid content of grass silages could also be determined in the presence of histidine.The estimation of amines produced by the microbial decomposition of herbage proteins during ensiling has previously involved their initial separation from the amino acids followed by quantitative partition chromatography. An alternative method for the estimation of these amines by ion-exchange chromatography on a weak cation-exchange resin is described. This method permits the colorimetric determination of β-phenylethylamine, tyramine, tryptamine, 5-hydroxytryptamine, putrescine, cadaverine and histamine without interference from the amino acids. The efficiency of this technique has been investigated using standard solutions of the naturally occurring amines and samples of good quality and of high pH spoilt silages.

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