Direct location of amino acid phenylthiohydantoins on paper chromatograms with ultraviolet light

1967 ◽  
Vol 21 (3) ◽  
pp. 472-474 ◽  
Author(s):  
Hubert Pirkle
Keyword(s):  
Amino Acid ◽  
Ultraviolet Light ◽  
Direct Location

scholarly journals CONSTITUENTS OF ELEMENTARY BODIES OF VACCINIA

1941 ◽  
Vol 74 (2) ◽  
pp. 133-144 ◽  
Author(s):  
Charles L. Hoagland ◽  
S. M. Ward ◽  
Joseph E. Smadel ◽  
Thomas M. Rivers
Keyword(s):  
Amino Acid ◽  
Ultraviolet Light ◽  
Flavin Adenine Dinucleotide ◽  
Specific Protein ◽  
Microbiological Assay ◽  
Acid Oxidase ◽  
Animal Cells ◽  
Oxidative Deamination ◽  
Amino Acid Oxidase ◽  
Chromatographic Methods

Suspensions of purified elementary bodies of vaccinia exhibit fluorescence in the presence of ultraviolet light. This fluorescent constituent can be separated by chromatographic methods provided the virus is first denatured by acid and heat. By means of the specific protein of d-amino acid oxidase it has been possible to identify the flavin constituent as flavin-adenine-dinucleotide and show that it can participate in the oxidative deamination of d-alanine. By means of microbiological assay the flavin component has been quantitatively measured and shown to compare favorably in concentration with that observed in animal cells and in some bacteria; its concentration in virus is lower than that observed in yeast. The demonstration that it exists as an integral portion of the virus is not conclusive. So far, however, it has been separated from the elementary bodies only by means which in themselves inactivate the virus.

Photochemical abiotic synthesis of amino-acid precursors from simulated planetary atmospheres by vacuum ultraviolet light

2005 ◽  
Vol 98 (2) ◽  
pp. 024907 ◽  
Author(s):  
Jun-ichi Takahashi ◽  
Hitomi Masuda ◽  
Takeo Kaneko ◽  
Kensei Kobayashi ◽  
Takeshi Saito ◽  
...  
Keyword(s):  
Amino Acid ◽  
Ultraviolet Light ◽  
Vacuum Ultraviolet ◽  
Planetary Atmospheres ◽  
Abiotic Synthesis ◽  
Amino Acid Precursors

Photolysis of pyridinoline, a cross-linking amino acid of collagen, by ultraviolet light

1982 ◽  
Vol 60 (5) ◽  
pp. 525-529 ◽  
Author(s):  
Sachiko Sakura ◽  
Daisaburo Fujimoto ◽  
Kikuo Sakamoto ◽  
Akio Mizuno ◽  
Katsutoshi Motegi
Keyword(s):  
Amino Acid ◽  
Ultraviolet Light ◽  
Alkaline Solution ◽  
Absorption Maximum ◽  
Acidic Solution ◽  
Cross Linking ◽  
Neutral Solution ◽  
Pyridinium Ring ◽  
Optimum Wavelength ◽  
Amino Acid Analyser

Pyridinoline, a cross-linking amino acid of collagen, was degraded by irradiation of ultraviolet light. The decomposition rate varied with pH of the solution and wavelength of irradiation light. The maximum of the degradation rate at individual pH coincides with the ultraviolet absorption maximum. Namely, it was maximally degraded by irradiation at 295 nm in acidic solution and at 325 nm in neutral and alkaline solution. At the optimum wavelength, the photolysis occurred more rapidly in neutral and alkaline solution than in acidic solution. The quantum yield in neutral solution was approximately 0.11 and independent of wavelength. One of the photolysis products was identified as hydroxylysine on an amino acid analyser, indicating that the cleavage of the pyridinium ring occurred.

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