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3. [Paper chromatographic amino acids analysis of natural compounds].

Author

Schröder I

Subjects
Arginine analysis, Chemistry Techniques, Analytical, Cystine analysis, Histidine analysis, Isoleucine analysis, Leucine analysis, Lysine analysis, Methionine analysis, Methods, Oxidation-Reduction, Phenylalanine analysis, Threonine analysis, Tryptophan analysis, Tyrosine analysis, Valine analysis, Amino Acids analysis, Chromatography, Paper, Proteins administration & dosage, Solvents
Published
1967

6. Amino acid chalcogen analogues as tools in peptide and protein research.

Author

Moroder L and Musiol HJ

Subjects
Animals, Crystallography, X-Ray, HSP70 Heat-Shock Proteins chemistry, HSP90 Heat-Shock Proteins chemistry, Humans, Immunoglobulin M chemistry, Protein Domains, Amino Acids chemistry, Chalcogens chemistry, Peptides chemistry, Proteins chemistry
Abstract

The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium element. In the methionine series, only the sulfur-containing methionine is a proteinogenic amino acid, while selenomethionine and telluromethionine are natural amino acids that are incorporated into proteins most probably because of the tolerance of the methionyl-tRNA synthetase; so far, methoxinine the oxygen analogue has not been discovered in natural compounds. Similarly, the chalcogen analogues of tryptophan and phenylalanine in which the benzene ring has been replaced by the largely isosteric thiophene, selenophene, and more recently, even tellurophene are fully synthetic mimics that are incorporated with more or less efficiency into proteins via the related tryptophanyl- and phenylalanyl-tRNA synthetases, respectively. In the serine/cysteine series, also selenocysteine is a proteinogenic amino acid that is inserted into proteins by a special translation mechanism, while the tellurocysteine is again most probably incorporated into proteins by the tolerance of the cysteinyl-tRNA synthetase. For research purposes, all of these natural and synthetic chalcogen amino acids have been extensively applied in peptide and protein research to exploit their different physicochemical properties for modulating structural and functional properties in synthetic peptides and rDNA expressed proteins as discussed in the following review., (© 2019 The Authors. Journal of Peptide Science published by European Peptide Society and John Wiley & Sons Ltd.)

Published
2020
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10. [Paper chromatographic amino acids analysis of natural compounds]

Author

I, Schröder

Subjects
Threonine, Chromatography, Paper, Lysine, Phenylalanine, Tryptophan, Proteins, Valine, Arginine, Chemistry Techniques, Analytical, Methionine, Leucine, Methods, Solvents, Cystine, Tyrosine, Histidine, Amino Acids, Isoleucine, Oxidation-Reduction
Published
1967

13. [Protein and amino acid composition of newborn rats under defective nutritional conditions].

Author

Ruiz-Torres A, Burmeister H, and Kürten I

Subjects
Animals, Animals, Newborn, Body Weight, Diet, Protein Deficiency, Rats, Amino Acids analysis, Proteins analysis
Abstract

The law protein nutrition of the nursing rat inhibits the growth of the new born rats. A percentage reduction of the dry substances by decrease of N2-free substances takes place. In relation to g dry substance the body protein content, collagen also, rises. Absolutely, these parts rest unaltered, just so the relation of the parenchymatous protein to collagen. The often support of view that starving provokes a collagen formation of the body, that means an exceed of the framework, can not be confirmed. Though in this paper we can give an explanation for the occurrence of this conclusion. Long interuptions of lactation periods remarkably have no effect on the growth and on the amin compartments of the body of new born rats. Only tryptophane is reduced in favour of the serine-fraction in the body of those animals. We discuss this finding as a change of the metabolisme of tryptophane depending of stress.

Published
1975
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18. [The alimentary ingestion, analysis and biological significance of thiocyanate]

Author

W, Weuffen, C, Franzke, and B, Thürkow

Subjects
Animals, Biological Transport, Active, Humans, Proteins, Amino Acids, Plants, Food Analysis, Thiocyanates
Abstract

A survey is given of the alimentary ingestion, metabolization and elimination as well as of the biological significance of thiocyanate (SCN-) in the mammalian organism. SCN- is an important nutritional factor since it influences essential bodily functions, e.g. immune response. Its analytical determination in vegetable and animal foodstuffs may be considerably affected by the reversible binding of SCN- to protein molecules and by natural products, e.g. amino acids and cyanide, from glycosidic precursors, which interfere with the reaction with bromine. This will be combining paper chromatography with gas chromatography. Except Brassica species which are relatively high in SCN- in glycosidic combination, vegetable foodstuffs contain nearly 0.1-1.3 mg SCN-/kg fresh material; animal foodstuffs, e.g. beef, contains 0.5-0.7 mg SCN-/kg. Balances calculations have shown that in non-smokers the average alimentary ingestion ranges from 1.8 to 5.2 mg SCN-/d.

Published
1984

19. [The cytospectrophotometrical determination of proteins by the tetrazonium coupling reaction. I. Optimization of the staining method (author's transl)]

Author

G, Nöhammer

Subjects
Liver, Staining and Labeling, Spectrophotometry, Animals, Proteins, Tetrazolium Salts, Lymphocytes, Amino Acids, Buffers, Hydrogen-Ion Concentration, Chickens, Cell Line
Abstract

The tetrazonium coupling reaction using Fast blue salt B and the sodium salt of 6-hydroxy-naphthalinsulfonic acid-(2) serves as a method for histochemical demonstration of proteins. Fast blue salt B reacts with histidin, tyrosin and in a slighter extent also with tryptophan. It is shown in this paper, that the histochemical tetrazonium reaction carried out under the optimal conditions is a specific staining for proteins and highly reproducible. The maximum of absorption at lambda = 530 nm of the azo dyes generated by the coupling reaction followes the Lambert-Beer's law. Nucleic acids as well as protein-SH-groups do not react with Fast blue salt B under the conditions described. Due to the exact reproducibility and specifity the tetrazonium coupling reactions seems to be a suitable method for at least comparative, microspectrometric protein determination within one species of cells.

Published
1978

20. [Protein and amino acid composition of newborn rats under defective nutritional conditions]

Author

A, Ruiz-Torres, H, Burmeister, and I, Kürten

Subjects
Animals, Newborn, Protein Deficiency, Body Weight, Animals, Proteins, Amino Acids, Diet, Rats
Abstract

The law protein nutrition of the nursing rat inhibits the growth of the new born rats. A percentage reduction of the dry substances by decrease of N2-free substances takes place. In relation to g dry substance the body protein content, collagen also, rises. Absolutely, these parts rest unaltered, just so the relation of the parenchymatous protein to collagen. The often support of view that starving provokes a collagen formation of the body, that means an exceed of the framework, can not be confirmed. Though in this paper we can give an explanation for the occurrence of this conclusion. Long interuptions of lactation periods remarkably have no effect on the growth and on the amin compartments of the body of new born rats. Only tryptophane is reduced in favour of the serine-fraction in the body of those animals. We discuss this finding as a change of the metabolisme of tryptophane depending of stress.

Published
1975