The ninhydrin-thiocarbohydrazide-silver proteinate reaction with proteins.

Malinin, George I.; Lo, H. K.; Malinin, Theodore I.

doi:10.1177/39.5.2016517

Cited by 3 publications

(4 citation statements)

References 2 publications

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“…The discovery of the ninhydrin-Schiff staining technique stimulated widespread interest in applying the method to histochemistry. Examples include studies of (a) a ninhydrin-specific chemical test for hair keratin (219), (b) energy and amino acid metabolism in mouse brain (220), (c) protein and DNA content of cells (221), (d) the cytochemistry of hepatic lysosomes and their enzymatic aggregates by a ninhydrin-DMSO-thiosemicabazide silver protein reaction (222), and (d) the use of a ninhydrin reagent to assess histochemically protein-bound amino acids in rat tissues (223). The DMSO-H 2 O mixed solvent enhanced the rate of oxidative deamination and favored specific staining of tissues (222).…”

Section: Forensic and Biomedical Sciencesmentioning

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.

522

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: Forensic and Biomedical Sciencesmentioning

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.

522

329

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“…Ninhydrin has become the universal reagent for the chemical development of latent fingerprints on porous surfaces such as paper 6–10. To enhance the usefulness of the ninhydrin method in forensic science, several attempts 11–14 have been made including the use of aqueous–organic mixed solvents as well as addition of surfactants. As the ninhydrin reaction results in decarboxylative deamination of amino acids to an aldehyde, the DMSO–water mixed solvent system enhanced the rate of oxidative deamination and favored specific staining of tissues 12.…”

Section: Introductionmentioning

confidence: 99%

“…To enhance the usefulness of the ninhydrin method in forensic science, several attempts 11–14 have been made including the use of aqueous–organic mixed solvents as well as addition of surfactants. As the ninhydrin reaction results in decarboxylative deamination of amino acids to an aldehyde, the DMSO–water mixed solvent system enhanced the rate of oxidative deamination and favored specific staining of tissues 12. Although some qualitative information is available on the role of organic solvents 8,13, kinetic evidence to distinguish their role is limited.…”

Section: Introductionmentioning

confidence: 99%

Micelle‐catalyzed reaction of ninhydrin with DL‐valine in the absence and presence of organic solvents

Kabir-ud-Din

Fatma

Khan

2006

Int J of Chemical Kinetics

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Kinetics of the DL-valine-ninhydrin reaction has been studied spectrophotometrically under varying conditions of [CTAB], [ninhydrin], [DL-valine], pH, temperature, and %(v/v) organic solvents (solvents used: 1-propanol, methylcellosolve, acetonitrile, and dimethyl sulfoxide). Addition of CTAB and increase in the proportion of organic solvents, both showed catalyzing effect on the reaction. The effect of simultaneous presence of CTAB and DMSO in the reaction mixture has also been seen. The rate profiles obtained for solutions containing from 10% to 70% DMSO exhibited clear maxima that shifted progressively to higher concentrations of CTAB. The experimental results are explained in terms of specific solvent effects and the formation of stoichiometric hydrate DMSO · 2H 2 O and the inhibitory effect of DMSO on micelle formation.

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“…Mesophase organizations of the ECM fibers can play important roles not only in the optimization of mechanical properties of the tissue itself, but also in the regulations of functions of embedded cells [ 65 ]. The assembly structure of oriented collagen fibers in consecutive layers with a finite twist angle (a variation of the twisted plywood structure) is the most common arrangement found in hydrated soft connective tissues in vertebrates [ 66 ] and bears a strong resemblance to the cholesteric order.…”

Section: Reviewmentioning

confidence: 99%

Liquid-crystalline nanoarchitectures for tissue engineering

Sung¹,

Kim²

2018

Beilstein J. Nanotechnol.

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Hierarchical orders are found throughout all levels of biosystems, from simple biopolymers, subcellular organelles, single cells, and macroscopic tissues to bulky organs. Especially, biological tissues and cells have long been known to exhibit liquid crystal (LC) orders or their structural analogues. Inspired by those native architectures, there has recently been increased interest in research for engineering nanobiomaterials by incorporating LC templates and scaffolds. In this review, we introduce and correlate diverse LC nanoarchitectures with their biological functionalities, in the context of tissue engineering applications. In particular, the tissuemimicking LC materials with different LC phases and the regenerative potential of hard and soft tissues are summarized. In addition, the multifaceted aspects of LC architectures for developing tissue-engineered products are envisaged. Lastly, a perspective on the opportunities and challenges for applying LC nanoarchitectures in tissue engineering fields is discussed. 205

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The ninhydrin-thiocarbohydrazide-silver proteinate reaction with proteins.

Cited by 3 publications

References 2 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

Micelle‐catalyzed reaction of ninhydrin with DL‐valine in the absence and presence of organic solvents

Liquid-crystalline nanoarchitectures for tissue engineering

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