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Why egg albumin and casein did not react ninhydrin reagent?
Egg albumin and casein are proteins that do not contain sufficient free amino groups to react with ninhydrin reagent, which detects free amino groups by forming a purple color complex. This may be due to the specific protein structure and the presence of amino acids that do not easily react with ninhydrin.
Why doesn't ninhydrin react with polypeptides?
Ninhydrin does react with polypeptides, specifically with the amino group of amino acids present in the polypeptide chain. This reaction leads to the formation of a colored compound that can be used for detection and analysis of amino acids and polypeptides.
Does ninhydrin has flaws?
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.
When glycine and alanine react what type of compound is formed?
When glycine and alanine react, a dipeptide compound is formed. This is because the amino acids join together through a peptide bond, which links the carboxyl group of one amino acid to the amino group of the other, creating a bond between the two amino acids.
Is ninhydrin the same as super glue?
No, ninhydrin is a chemical compound used to detect the presence of amino acids, while super glue is a brand name for cyanoacrylate adhesive. They have different chemical compositions and purposes.
Why egg albumin and casein did not react ninhydrin reagent?
Egg albumin and casein are proteins that do not contain sufficient free amino groups to react with ninhydrin reagent, which detects free amino groups by forming a purple color complex. This may be due to the specific protein structure and the presence of amino acids that do not easily react with ninhydrin.
Why doesn't ninhydrin react with polypeptides?
Ninhydrin does react with polypeptides, specifically with the amino group of amino acids present in the polypeptide chain. This reaction leads to the formation of a colored compound that can be used for detection and analysis of amino acids and polypeptides.
Does ninhydrin has flaws?
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.
What color develops when ninhydrin react with amino acids?
These are the amino acids that will yield positive result to the ninhydrin test: Non-polar amino acids: Glycine, Alanine, Valine, Leucine, Isoleucine, Phenylalanine, Methionine, Tryptophan Polar Neutral Amino acids: Serine, Cysteine, Threonine, Asparagine, Glutamine, Tyrosine Polar Acidic Amino Acids: Aspartic acid and Glutamic acid Polar Basic Amino Acids: Histidine, Lysine, Arginine
Would the ninhydrin test be useful and reliable for showing the presence or the absence of proteins?
Yes, the ninhydrin test is useful for detecting the presence of proteins because it reacts with amino acids to produce a colored product. However, it may not be reliable for determining the absence of proteins due to possible interference from other substances that can also react with ninhydrin.
What questions have been raised about ninhydrin?
Ninhydrin is a chemical used to expose latent fingerprints, but its use is declining because of the slow reaction time it takes for it to react with the oil in the fingerprints. You can use heat to speed the process up but there are other faster options.
What functional group must be present for the ninhydrin test to work?
The ninhydrin test requires the presence of a primary or secondary amine functional group to react with ninhydrin, resulting in a color change to blue or purple. Tertiary amines do not react with ninhydrin in this way.
When glycine and alanine react what type of compound is formed?
When glycine and alanine react, a dipeptide compound is formed. This is because the amino acids join together through a peptide bond, which links the carboxyl group of one amino acid to the amino group of the other, creating a bond between the two amino acids.
What substance is found in human skin that reacts with ninhydrin resulting to stain?
Amino acids, specifically the primary amine group found in proteins, react with ninhydrin to produce a purple-blue color. This reaction is commonly used to detect and visualize amino acids in biological samples such as human skin.
How is the reduction of plasma alanine concentration caused by gluconeogenesis?
During gluconeogenesis, alanine is converted into pyruvate and then used in the process to produce glucose. This results in a decrease in plasma alanine concentration as the alanine molecules are utilized for energy production.
In the glucose alanine cycle how much glucose production does alanine account for?
1.0 gram of alanine accounts for the production of approximately 0.681 grams of glucose in the glucose-alanine cycle.
What group in amino acids or proteins in general is responsible for the ninhydrin reaction?
The amino group (-NH2) present in the amino acids/proteins is responsible for the ninhydrin reaction. Ninhydrin reacts with this group to form a colored compound, which is used in assays to detect amino acids.
