Electron paramagnetic resonance study of free radical products of the reaction of ninhydrin with amino acids, peptides and proteins

Yuferov, Vadim; Froncish, Woiciech; Kharitonenkov, I G; Kalmanson, A.E.

doi:10.1016/0005-2795(70)90054-1

Cited by 5 publications

(4 citation statements)

References 4 publications

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“…Free Radical Products. Ninhydrin reacts with amino acids to produce free radicals characteristic of various amino acids as well as of N-terminal amino acids in peptides and proteins (55,164,165) (Figure 5). Related studies indicate that ninhydrin also participates in solid-state cascade reactions with proline (166) and that the photochemistry of ninhydrin is solventdependent (167).…”

Section: Chemistry and Mechanisms Of Ninhydrin Reactionsmentioning

confidence: 99%

Applications of the Ninhydrin Reaction for Analysis of Amino Acids, Peptides, and Proteins to Agricultural and Biomedical Sciences

Friedman

2004

J. Agric. Food Chem.

529

329

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The reaction of ninhydrin with primary amino groups to form the purple dye now called Ruhemann's purple (RP) was discovered by Siegfried Ruhemann in 1910. In addition, imines such as pipecolic acid and proline, the guanidino group of arginine, the amide groups of asparagine, the indole ring of tryptophan, the sulfhydryl group of cysteine, amino groups of cytosine and guanine, and cyanide ions also react with ninhydrin to form various chromophores of analytical interest. Since its discovery, extensive efforts have been made to apply manual and automated ninhydrin reactions as well as ninhydrin spray reagents to the detection, isolation, and analysis of numerous compounds of interest across a broad spectrum of disciplines. These include agricultural, biochemical, clinical, environmental, food, forensic, histochemical, microbiological, medical, nutritional, plant, and protein sciences. This reaction is unique among chromogenic reactions in that at pH 5.5 it results in the formation of the same soluble chromophore by all primary amines which react, be they amines, amino acids, peptides, proteins, and even ammonia. Because the chromophore is not chemically bound to the protein or other insoluble material, it is not lost when the insoluble substrate is removed by centrifugation or filtration after the reaction is completed. The visible color of the chromophore is distinctive and is generally not affected by the yellow colors present in many food, plant, and tissue extracts. Adaptations of the classical ninhydrin reaction to specialized needs in analytical chemistry and biochemistry include the use of acid, alkaline, and fluorogenic ninhydrin reagents. To cross-fertilize information among several disciplines wherein an interest in the ninhydrin reaction has developed, and to enhance its utility, this review attempts to integrate and correlate the widely scattered literature on ninhydrin reactions of a variety of structurally different compounds. Specifically covered are the following aspects: historical perspective, chemistry and mechanisms, applications, and research needs. A better understanding of these multifaceted ninhydrin reactions provide a scientific basis for further improvements of this important analytical technique.

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Section: Chemistry and Mechanisms Of Ninhydrin Reactionsmentioning

confidence: 99%

Applications of the Ninhydrin Reaction for Analysis of Amino Acids, Peptides, and Proteins to Agricultural and Biomedical Sciences

Friedman

2004

J. Agric. Food Chem.

529

329

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“…Free radicals formed by the reaction of ninhydrin with primary alkyl amine.~ in ethanol (Radical 1) The reaction mixtures of ninhydrin with primary amines readily colored deep purple even at room temperature, and simultaneously gave rise to development of the esr spectra with characteristic hyperfine structure.…”

Section: Resultsmentioning

confidence: 99%

“…There have been few studies on the free radical formation by the reaction of ninhydrin with amino compounds, i.e., with amino acids 1 ) and alkyl amines.…”

mentioning

confidence: 99%

Free Radicals Formed by the Reaction of Ninhydrin with Alkyl Amines

Hayashi¹,

Hirata²,

Yano³

et al. 1978

Agricultural and Biological Chemistry

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“…There have been a number of studies on this color development; recently the structure and the mechanism of formation of the red pigment have been proposed (Kurata et al, 1973; Ranganna and Setty, 1974). Additionally, there have been some studies on the development of free-radical products in the reaction of amino compounds with carbonyl compounds relating to ascorbic acid, for example, the stable radicals in melanoidin as the browning reaction products from glucose and glycine (Mitsuda et al, 1965), the unstable free radicals in the reaction of ninhydrin with amino compounds (Orr, 1965;Yeferov et al, 1970), and a radical intermediate in a redox reaction between ascorbic acid and dehydroascorbic acid (Laroff et al, 1972).…”

mentioning

confidence: 99%

Formation of free-radical products by the reaction of dehydroascorbic acid with amino acids

Yano¹,

Hayashi²,

Namiki³

1976

J. Agric. Food Chem.

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Electron paramagnetic resonance study of free radical products of the reaction of ninhydrin with amino acids, peptides and proteins

Cited by 5 publications

References 4 publications

Applications of the Ninhydrin Reaction for Analysis of Amino Acids, Peptides, and Proteins to Agricultural and Biomedical Sciences

Applications of the Ninhydrin Reaction for Analysis of Amino Acids, Peptides, and Proteins to Agricultural and Biomedical Sciences

Free Radicals Formed by the Reaction of Ninhydrin with Alkyl Amines

Formation of free-radical products by the reaction of dehydroascorbic acid with amino acids

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