No because it doesn't contain aromatic group
I reckon the answer would be that phenol has a hydroxyl group (-OH) which is bonded to a phenyl ring. It yields the same positive result like tyrosine which has a hydroxyl group bonded to its phenyl ring.
The xanthoproteic test is used to detect the presence of aromatic amino acids, particularly tyrosine and tryptophan, by turning yellow upon reaction with nitric acid. Samples that do not contain these amino acids, such as certain non-aromatic amino acids (e.g., glycine, alanine) or peptides and proteins lacking these residues, will not yield a positive test. Additionally, any substances that do not contain proteins or peptides, such as carbohydrates or lipids, will also not give a positive result. Thus, the absence of aromatic amino acids or proteins in the sample is the reason for a negative xanthoproteic test.
Phenylalanine. When phenylalanine is subjected to a xanthoproteic test, it will produce a yellow solution due to the reaction of the aromatic ring with nitric acid, indicating the presence of phenyl group in the tripeptide.
Yes, adrenaline gives a positive result in the xanthoproteic test. This test is used to detect the presence of aromatic amino acids, such as tyrosine and tryptophan, by reacting them with concentrated nitric acid, which produces a yellow coloration. Since adrenaline contains a phenolic structure derived from tyrosine, it reacts positively in this test, indicating the presence of these aromatic compounds.
The xanthoproteic test involves nitration of aromatic amino acids in proteins, which may not always be specific for proteins as other compounds containing these amino acids can give false positive results. The Millon-Nasse test is based on the reaction of phenol groups in proteins, which can also react with other substances containing phenol groups, leading to false positive results. Overall, these tests lack specificity and can give inaccurate results when used to examine proteins.
No, adrenaline will not give a positive xanthoproteic test. The xanthoproteic test is used to detect the presence of proteins, not hormones like adrenaline. Adrenaline is a hormone that is involved in the body's fight-or-flight response, and it does not react in the same way as proteins do in the xanthoproteic test.
Phenylalanine gave a yellow to orange color in xanthoproteic test which means it is positive.
No, not all amino acids with an aromatic ring give a positive xanthoproteic test. The xanthoproteic test is mainly positive for amino acids containing aromatic rings with phenolic groups such as tyrosine and phenylalanine. Aromatic amino acids like tryptophan do not give a positive xanthoproteic test under identical conditions.
I reckon the answer would be that phenol has a hydroxyl group (-OH) which is bonded to a phenyl ring. It yields the same positive result like tyrosine which has a hydroxyl group bonded to its phenyl ring.
The xanthoproteic test is used to detect the presence of aromatic amino acids, particularly tyrosine and tryptophan, by turning yellow upon reaction with nitric acid. Samples that do not contain these amino acids, such as certain non-aromatic amino acids (e.g., glycine, alanine) or peptides and proteins lacking these residues, will not yield a positive test. Additionally, any substances that do not contain proteins or peptides, such as carbohydrates or lipids, will also not give a positive result. Thus, the absence of aromatic amino acids or proteins in the sample is the reason for a negative xanthoproteic test.
My son normally eats 10minutes after I give him insulin
Phenylalanine. When phenylalanine is subjected to a xanthoproteic test, it will produce a yellow solution due to the reaction of the aromatic ring with nitric acid, indicating the presence of phenyl group in the tripeptide.
Yes, adrenaline gives a positive result in the xanthoproteic test. This test is used to detect the presence of aromatic amino acids, such as tyrosine and tryptophan, by reacting them with concentrated nitric acid, which produces a yellow coloration. Since adrenaline contains a phenolic structure derived from tyrosine, it reacts positively in this test, indicating the presence of these aromatic compounds.
You have 'human Insulin' produced by a technique called as 'Genetic engineering'. In this you put 'Human gene' isolated from 'Human cells' into DNA of microorganism. They produce 'exact' replica of 'human insulin' and isextremelyuseful. It will never ever form antibody like Pig Insulin or Bovine insulin. But it has a dis-advantage of Pharmacokinetics. Given intro-venous or intramuscular it has half life of only about 8 minutes. So you have to give it either by continuous intro-venous drip or by repeated intro-muscular injections say every 10 to 15 minutes. For slow absorption, you have to give sub-cutaneous injection. Then it becomes too slow and you do not have a route in between. If you give subcutaneous injection of 'Human insulin', then there is immediate hyperglycemia, fallowed by hyperglycemia. So you have designers Insulin with there own disadvantages.
The xanthoproteic test involves nitration of aromatic amino acids in proteins, which may not always be specific for proteins as other compounds containing these amino acids can give false positive results. The Millon-Nasse test is based on the reaction of phenol groups in proteins, which can also react with other substances containing phenol groups, leading to false positive results. Overall, these tests lack specificity and can give inaccurate results when used to examine proteins.
No because it doesn't contain aromatic group
no from insulin but diabetes, liver disease, kidney infection may show up false positive on drug tests.