answersLogoWhite

0

yes

User Avatar

Hayden Tay

Lvl 3
4y ago

What else can I help you with?

Continue Learning about Chemistry

All amino acid having an aromatic ring give a positive xanthoproteic test under identical condition?

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.


What functional group gives a positive test in the xanthoproteic test?

The phenolic functional group gives a positive test in the xanthoproteic test. This test involves the reaction of phenolic compounds with concentrated nitric acid, resulting in a yellow coloration due to the formation of nitrophenols.


Why is the xanthoproteic test for phenol negative?

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.


Which halogens give a positive beilstein test?

Chlorine, bromine, and iodine give a positive Beilstein test. The test involves ignition of a compound in the presence of copper oxide, which forms a green flame due to the halogen present in the compound.


Does phenol give a positive biuret test?

No, phenol does not give a positive biuret test. The biuret test is used to detect the presence of proteins, not phenol. Phenol is a type of organic compound that does not contain the peptide bonds that the biuret test reacts with.

Related Questions

Do you expect adrenaline to give a positive xanthoproteic test?

No, adrenaline is not expected to give a positive xanthoproteic test. The xanthoproteic test is used to detect the presence of proteins containing aromatic amino acids, which react with nitric acid to form a yellow-colored compound. While adrenaline does contain an aromatic ring, it is classified as a catecholamine, not a protein, and therefore does not typically produce a positive result in this test.


Does adrenaline give a positive result in xanthoproteic?

Yes, adrenaline can give a positive result in the xanthoproteic test. This test identifies proteins containing aromatic amino acids, such as phenylalanine and tyrosine, which are present in adrenaline. When the adrenaline is heated with concentrated nitric acid, it forms a yellow-colored compound, indicating a positive result.


Would adrenaline give a positive test to Xanthoproteic test?

Yes, adrenaline would give a positive result in the Xanthoproteic test. The test detects aromatic amino acids and compounds, and adrenaline contains a phenolic group, which reacts with nitric acid to form yellow-colored nitrophenol derivatives. This reaction indicates the presence of these aromatic compounds, thus confirming a positive result.


Does adrenaline give a positive result to xanthoproteic test?

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.


Why phenylalanine give negative result with xanthoproteic test?

Phenylalanine gave a yellow to orange color in xanthoproteic test which means it is positive.


Is albumin positive to xanthoproteic test?

Yes, albumin is positive to the xanthoproteic test. The xanthoproteic test is used to detect the presence of proteins containing aromatic amino acids, such as albumin, by forming a yellow color when treated with nitric acid.


All amino acid having an aromatic ring give a positive xanthoproteic test under identical condition?

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.


Does human insulin give positive xanthoproteic test?

No because it doesn't contain aromatic group


What tripeptide will give a positive 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.


What samples did not give a positive test with xanthoproteic test why?

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.


Do albumin gives a positive xanthoproteic test?

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.


Why are xanthoproteic and millon-nasse test unsatisfactory for the use in examination for proteins?

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.