Well, the best I could come up with is it's either:C9H6O2orC4H3O2If someone knows any different please correct me.jman63: it is actually C9H6O4
Yes, ninhydrin has some drawbacks. It can react with other substances present in the sample, leading to false positive results. Additionally, the reaction with ninhydrin is not specific to a particular amino acid, which can limit its application in identifying specific amino acids.
NO, ninhydrin is not the same as super glue
The boiling point of ninhydrin is approximately 275-280°C.
Ninhydrin reagent is prepared by dissolving ninhydrin powder in a solvent such as ethanol or acetone. The solution is typically heated gently to aid dissolution. It is important to prepare fresh ninhydrin reagent before use to ensure its effectiveness in detecting amino acids.
Since amino acids are colourless compounds, ninhydrin is used for detecting them. To identify this, after development, the TLC plate is sprayed with ninhydrin reagent and dried in an oven, at 105°C for about 5 minutes. Ninhydrin reacts with α- amino acids that results in purple coloured spots [(due to the formation of the complex - Rheuman's purple).
No! because the Ninhydrin test is mostly used to detect ammonia or primary secondary amines
Ninhydrin reacts with amino acids present in the sweat from fingerprints, producing a purple or blue color. This allows for the visualization and development of latent fingerprints on surfaces.
The principle of the ninhydrin test is based on the reaction of ninhydrin with amino acids or proteins to form a purple or blue color complex. This test is commonly used to detect the presence of amino acids in a sample, making it a useful tool in protein analysis and forensic science.
No, Ninhydrin is not used to test for the presence of lipids. Ninhydrin is commonly used to detect the presence of amino acids or proteins by producing a purple color when in contact with them. Lipids are usually tested using methods like the Sudan Red test or the paper towel test.
In the ninhydrin reaction, ammonia gas (NH₃) is liberated. This reaction is commonly used to detect amino acids and proteins, as ninhydrin reacts with the free amino groups, leading to the formation of a colored product and the release of ammonia. The presence of ammonia can be observed as a byproduct during the reaction process.
Ninhydrin works because it reacts with the amino acids left behind in a latent print. Ninhydrin has a polar carbonyl carbon with is electron deficient. It is attacked by the nucleophilic nitrogren on an amino acid, temporarily combining the ninhydrin and amino acid molecule. The structure is rearranged until the origionally attacked carbon is protonated and leaves in the form of water. This creates a schiff base when the nitrogen is double bonded to the origionally attacked carbon. This molecule rearranges again so that the nitrogen is double bonded to the adjacent carbon of the amino acid. This last rearrangement produces carbon dioxide gas. Further rearrangement of the product produces ruheman's purple.