scholarly journals Amino Acids and Protein Synthesis in Developing Wheat Endosperm

1963 ◽  
Vol 16 (2) ◽  
pp. 384 ◽  
Author(s):  
AC Jennings ◽  
RK Morton

The amino acid composition of several protein fractions of developing wheat endosperm (cv. Gabo, grown in 1960 in Adelaide) was determined by ion-exchange chromatography. There were considerable differences in the compositions of the fractions extracted by pyrophosphate, acetic acid, and by sodium hydroxide. The composition of the fraction extracted by acetic acid remained relatively constant during development whereas there were changes in the compositions of the fractions extracted by pyrophosphate buffer, and by sodium hydroxide.

1969 ◽  
Vol 52 (5) ◽  
pp. 981-984 ◽  
Author(s):  
J E Knipfel ◽  
D A Christensen ◽  
B D Owen

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 < 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.


1976 ◽  
Vol 29 (2) ◽  
pp. 11 ◽  
Author(s):  
Robert C Marshall ◽  
JM Gillespie

The present paper continues the study of the reduced and S-carboxymethylated high-sulphur proteins from mouse hair. Fractions have been obtained in a substantially purified form by fractional precipitation with ammonium sulphate at pH 6, followed by ion exchange chromatography on cellulose phosphate at pH 2�6. Approximately 80% by weight of the high-sulphur proteins fall into the ultra-high-sulphur category (carboxymethyicysteine content greater than 26 residues per 100 residues), and they cover a molecular weight range of 17000-28000. The components show a remarkable diversity in amino acid composition; for example the contents of arginine and glycine each vary by about 3 : 1. The remainder of the proteins contain 17-20 residues per 100 residues of carboxymethyicysteine, are smaller in size (molecular weight 11 500), and also show great diversity in overall amino acid composition.


1970 ◽  
Vol 48 (3) ◽  
pp. 386-388 ◽  
Author(s):  
M. Yaguchi ◽  
M. B. Perry

An amino acid analyzer is used to separate seven 2-ammo-2-deoxy-D-hexoses (allosamine, altrosamine, glucosamine, mannosamine, gulosamine, galactosamine, and talosamine). A borate citrate buffer at pH 7.24 is used at 60 °C. Acidic and neutral amino acids, if present, are eluted before any of the hexosamines.


2017 ◽  
Vol 63 (3) ◽  
pp. 266-271 ◽  
Author(s):  
T.N. Pogorelova ◽  
V.O. Gunko ◽  
V.V. Avrutskaya ◽  
L.V. Kaushanskaya ◽  
O.A. Durnitsyna

The content of the amino acids in the placenta during physiological pregnancy and fetal growth restriction (FGR) has been investigated my means of the method of ion-exchange chromatography. It has been found that in FGR the placental amino acid pool is characterized by a decreased content of arginine, proline, alanine, serine, cysteine, methionine, tryptophan, leucine, threonine, tyrosine, phenylalanine, glutamine and an increased content of dicarboxylic amino acids, lysine, histidine and glycine. These changes are accompanied by altered activity of some enzymes of amino acid metabolism, and the degree of these changes correlates with the level of corresponding amino acids.


Blood ◽  
1960 ◽  
Vol 16 (5) ◽  
pp. 1564-1571 ◽  
Author(s):  
DAVID W. ALLEN

Abstract 1. The concentrations of certain amino acids were measured by ion exchange chromatography in mature red cells, in red cells with a high percentage of reticulocytes, and in the plasma in which these red cells had been suspended. The concentration ratio as a measure of net accumulation of the red cells for amino acids was derived from these data. 2. Adult red cells can accumulate glycine and alanine, but not methionine, valine, isoleucine or leucine. 3. Reticulocytes can accumulate glycine best, then alanine, then methionine, isoleucine, and leucine to approximately the same extent. They were unable to maintain a concentration gradient for valine. 4. In two patients with thalassemia, no abnormality was found in the plasma or red cell levels of citrulline, proline, glycine, alanine, valine, isoleucine, tyrosine, or phenylalanine. In one of the thalassemic patients no abnormality of histidine was found. The amino acid accumulation by thalassemic, or fetal red cells was the same as for normal red cells of comparable reticulocyte percentage.


1957 ◽  
Vol 10 (3) ◽  
pp. 384 ◽  
Author(s):  
RA Weller

Samples of bacteria and of protozoa were separated from the rumen fluids of sheep which had been fed four different types of ration. Amino acid analyses by ion-exchange chromatography were performed on hydrolysates of "whole protein" preparations of the microbial fractions.


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