Reactions of aqueous chlorine dioxide with amino acids found in water

1979 ◽  
Vol 23 (1) ◽  
pp. 456-463 ◽  
Author(s):  
Kevser Taymaz ◽  
David T. Williams ◽  
Frank F. Benoit
Keyword(s):  
Amino Acids ◽  
Chlorine Dioxide

Reaction of chlorine dioxide with amino acids and peptides: Kinetics and mutagenicity studies

1987 ◽  
Vol 188 (4) ◽  
pp. 259-266 ◽  
Author(s):  
Hsiou-kun Tan ◽  
Willis B. Wheeler ◽  
Cheng-i Wei
Keyword(s):  
Amino Acids ◽  
Chlorine Dioxide

Reactivity of chlorine dioxide with amino acids, peptides, and proteins

2012 ◽  
Vol 10 (3) ◽  
pp. 255-264 ◽  
Author(s):  
Virender K. Sharma ◽  
Mary Sohn
Keyword(s):  
Amino Acids ◽  
Chlorine Dioxide

Novel insights in chlorine dioxide based disinfection mechanism –Investigation of the reaction with amino acids

2022 ◽  
Author(s):  
Mischa Jütte ◽  
Janine Vanessa Große ◽  
Mohammad Sajjad Abdighahroudi ◽  
Christoph Schüth ◽  
Holger Volker Lutze
Keyword(s):  
Amino Acids ◽  
Chlorine Dioxide

This study systematically investigated the reactions of N-Acetyl-L-tyrosine (NAL tyrosine) and N-Acetyl-L-tryptophan (NAL-tryptophan) with ClO2 and FAC. NAL-tyrosine and NAL-tryptophan are examples of reactive amino acids included in peptides and...

A Kinetic Study of the Reaction of Aqueous Chlorine and Chlorine Dioxide with Amino Acids, Peptides and Proteins

1987 ◽  
Vol 52 (6) ◽  
pp. 1706-1711 ◽  
Author(s):  
H. TAN ◽  
A. C. SEN ◽  
W. B. WHEELER ◽  
J. A. CORNELL ◽  
C. I. WEI
Keyword(s):  
Amino Acids ◽  
Kinetic Study ◽  
Chlorine Dioxide

Chlorine dioxide reaction with selected amino acids in water

2009 ◽  
Vol 164 (2-3) ◽  
pp. 1089-1097 ◽  
Author(s):  
Sergio Navalon ◽  
Mercedes Alvaro ◽  
Hermenegildo Garcia
Keyword(s):  
Amino Acids ◽  
Chlorine Dioxide

Homochirality as the Signature of Extra-Terrestrial Life

1997 ◽  
Vol 161 ◽  
pp. 505-510
Author(s):  
Alexandra J. MacDermott ◽  
Laurence D. Barron ◽  
Andrè Brack ◽  
Thomas Buhse ◽  
John R. Cronin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Optical Rotation ◽  
Physical Origin ◽  
Natural Choice ◽  
Rosetta Mission ◽  
Terrestrial Life ◽  
Subsurface Layers ◽  
Solar System Bodies ◽  
Origin Of Homochirality

AbstractThe most characteristic hallmark of life is its homochirality: all biomolecules are usually of one hand, e.g. on Earth life uses only L-amino acids for protein synthesis and not their D mirror images. We therefore suggest that a search for extra-terrestrial life can be approached as a Search for Extra- Terrestrial Homochirality (SETH). The natural choice for a SETH instrument is optical rotation, and we describe a novel miniaturized space polarimeter, called the SETH Cigar, which could be used to detect optical rotation as the homochiral signature of life on other planets. Moving parts are avoided by replacing the normal rotating polarizer by multiple fixed polarizers at different angles as in the eye of the bee. We believe that homochirality may be found in the subsurface layers on Mars as a relic of extinct life, and on other solar system bodies as a sign of advanced pre-biotic chemistry. We discuss the chiral GC-MS planned for the Roland lander of the Rosetta mission to a comet and conclude with theories of the physical origin of homochirality.

Hydrogen Cyanide Polymers from the Impact of Comet P/Shoemaker-Levy 9 on Jupiter

1997 ◽  
Vol 161 ◽  
pp. 179-187
Author(s):  
Clifford N. Matthews ◽  
Rose A. Pesce-Rodriguez ◽  
Shirley A. Liebman
Keyword(s):  
Amino Acids ◽  
Solar System ◽  
Hydrogen Cyanide ◽  
Nitrogen Heterocycles ◽  
Laboratory Studies ◽  
Heterogeneous Solids ◽  
The Many ◽  
Comet Halley ◽  
The Impact ◽  
By Products

AbstractHydrogen cyanide polymers – heterogeneous solids ranging in color from yellow to orange to brown to black – may be among the organic macromolecules most readily formed within the Solar System. The non-volatile black crust of comet Halley, for example, as well as the extensive orangebrown streaks in the atmosphere of Jupiter, might consist largely of such polymers synthesized from HCN formed by photolysis of methane and ammonia, the color observed depending on the concentration of HCN involved. Laboratory studies of these ubiquitous compounds point to the presence of polyamidine structures synthesized directly from hydrogen cyanide. These would be converted by water to polypeptides which can be further hydrolyzed to α-amino acids. Black polymers and multimers with conjugated ladder structures derived from HCN could also be formed and might well be the source of the many nitrogen heterocycles, adenine included, observed after pyrolysis. The dark brown color arising from the impacts of comet P/Shoemaker-Levy 9 on Jupiter might therefore be mainly caused by the presence of HCN polymers, whether originally present, deposited by the impactor or synthesized directly from HCN. Spectroscopic detection of these predicted macromolecules and their hydrolytic and pyrolytic by-products would strengthen significantly the hypothesis that cyanide polymerization is a preferred pathway for prebiotic and extraterrestrial chemistry.

Methionine-Specific Staining of Collagen

1982 ◽  
Vol 40 ◽  
pp. 294-295
Author(s):  
E.M. Kuhn ◽  
K.D. Marenus ◽  
M. Beer
Keyword(s):  
Amino Acids ◽  
Collagen Fibers ◽  
Type Iii Collagen ◽  
Type I ◽  
Electron Microscopic ◽  
Good Correspondence ◽  
Specific Staining ◽  
Type Iii ◽  
Different Types ◽  
Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

Prevalence of the pit and antipit in the genus Glycine

1987 ◽  
Vol 45 ◽  
pp. 986-987
Author(s):  
R. W. Yaklich ◽  
E. L. Vigil ◽  
W. P. Wergin
Keyword(s):  
Amino Acids ◽  
Endoplasmic Reticulum ◽  
Glycine Max ◽  
Seed Coat ◽  
Cell Types ◽  
Abaxial Surface ◽  
Legume Seed ◽  
Initial Report ◽  
Cone Cells ◽  
Glycine Max L

The legume seed coat is the site of sucrose unloading and the metabolism of imported ureides and synthesis of amino acids for the developing embryo. The cell types directly responsible for these functions in the seed coat are not known. We recently described a convex layer of tissue on the inside surface of the soybean (Glycine max L. Merr.) seed coat that was termed “antipit” because it was in direct opposition to the concave pit on the abaxial surface of the cotyledon. Cone cells of the antipit contained numerous hypertrophied Golgi apparatus and laminated rough endoplasmic reticulum common to actively secreting cells. The initial report by Dzikowski (1936) described the morphology of the pit and antipit in G. max and found these structures in only 68 of the 169 seed accessions examined.

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