PHOTOMETRIC DETECTION OF AMINO ACID SARCOSINE USING ITS HYDROLYSIS BY SARCOSINE OXIDASE AND AMPLEX RED FLUOROPHORE

Abstract To improve accuracy and precision of amino acid analysis In 12 Dutch feed laboratories, a proficiency study was organized twice annually over a 4-year period. The method used included reflux acid hydrolysis for 22 h followed by evaporation, separation on a cation-exchange resin In an amino acid analyzer, and photometric detection after post-column derlvatlzatlon with ninhydrln. For the determination of sulfurcontaining amino acids, samples were oxidized prior to hydrolysis. For the determination of tryptophan, samples underwent an alkaline hydrolysis excluding oxygen, were separated by liquid chromatography on a Hypersil ODS analytical column, and were assayed by UV or fluorescence detection. The average relative standard deviations within (CVr) and between (CVR) laboratories were 3 and 7%, respectively. For some mixed feed samples, the results from the proficiency study were compared with those obtained by the International Analytical Group. For those samples, the relative standard deviation of the difference between IAG and Dutch groups was only 1.9%. For samples that were analyzed twice during this 4-year period, relative standard deviation of between-serles differences was only 2.1 %.

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Determination of sulfur-containing amino acid residues in proteins by pyrolysis-gas chromatography with flame photometric detection

Fresenius Zeitschrift für Analytische Chemie ◽

10.1007/bf00556916 ◽

1988 ◽

Vol 329 (7) ◽

pp. 781-785 ◽

Cited By ~ 3

Author(s):

Masahiro Ohsawa ◽

Hajime Ohtani ◽

Shin Tsuge

Keyword(s):

Gas Chromatography ◽

Amino Acid ◽

Amino Acid Residues ◽

Pyrolysis Gas ◽

Pyrolysis Gas Chromatography ◽

Photometric Detection ◽

Flame Photometric Detection ◽

Sulfur Containing

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Study of the amino acid composition of macaroni products under the influence of different storage temperatures

10.33920/igt-01-2102-11 ◽

2021 ◽

pp. 147-152

Author(s):

I.A. Tarasova ◽

E.A. Tarasova

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Comparative Method ◽

Exchange Chromatography ◽

Photometric Detection ◽

Three Samples ◽

C 30 ◽

Limiting Amino Acids

The article presents the studies of the amino acid composition in the samples of macaroni products by the method of chromatographic analysis. Amino acids were separated by ion exchange chromatography, reacted with ninhydrin, and their content was determined by photometric detection at a wavelength of 570 nm. Amino acid compositions of three samples of macaroni products stored at temperatures 20±2°C, 30±2°C and 40±2°C were investigated. The biological value of macaroni products proteins was determined by a comparative method for analyzing the quantitative content of amino acids with the ideal protein scale proposed by the FAO/WHO Committee. The limiting amino acids for macaroni products after 12 months of storage are valine, threonine and lysine, with the lysine content being the lowest.

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The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100142372 ◽

1986 ◽

Vol 44 ◽

pp. 150-151

Author(s):

M.K. Lamvik ◽

L.L. Klatt

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Staining Pattern ◽

Banding Patterns ◽

Mass Thickness ◽

New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

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Electron probe x-ray microanalysis and electron microscopy of amino acid absorption and transport by the small intestine: inhibition by chemical poisons and correlation to the elemental composition of the epithelial cells

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100142311 ◽

1986 ◽

Vol 44 ◽

pp. 134-135

Author(s):

A. J. Tousimis

Keyword(s):

Small Intestine ◽

Amino Acid ◽

Epithelial Cells ◽

Elemental Composition ◽

Isotope Labeling ◽

Structural Components ◽

X Ray ◽

Human Small Intestine ◽

Transport Studies

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.

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Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100147776 ◽

1993 ◽

Vol 51 ◽

pp. 388-389

Author(s):

Chi-Ming Wei ◽

Margaret Hukee ◽

Christopher G.A. McGregor ◽

John C. Burnett

Keyword(s):

Amino Acid ◽

Natriuretic Peptide ◽

Vascular Tone ◽

Cardiac Tissue ◽

Ring Structure ◽

Terminal Amino Acid ◽

Amino Acid Peptide ◽

Normal Human ◽

Terminal Amino ◽

The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

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