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What amino acids give positive Ehrlich test?
Amino acids that contain an indole group, such as tryptophan, give a positive Ehrlich test. The Ehrlich test is a colorimetric test that detects compounds containing indole or phenolic groups by producing a pink or red color when reacted with p-dimethylaminobenzaldehyde reagent.
What amino acids are found in nitroprusside test?
Nitroprusside test detects the presence of cysteine and cystine amino acids. These amino acids react with nitroprusside to form a purple color complex, indicating a positive test for cysteine or cystine.
What is the fate of amino group in the metabolism of amino acids for energy?
Excreted as urea. this was the answer for my test
Can you distinguish proteins and other amino compounds by the ninhyndrin test?
Because proteins are polymers of amino acids, hydrolysis followed by amino acids determination is a method. Ninhydrin is an oxidating agent which leads to the oxidative deamination of alpha-amino groups. Ninhyndrin test is used to detect ammonia, primary (deep blue or purple color (Ruhemann's purple)) and secondary amines (yellow), this is a proof of free amino acids in proteins. to distinguisn between Amino Acids and proteins you need a peptide bond test which can be done by Biuret test.
Are all amino acids reactive with the Biuret reagent?
Not all amino acids react with the Biuret reagent. The Biuret test specifically detects the presence of peptide bonds, which are formed when amino acids link together in proteins. Therefore, free amino acids without peptide bonds do not produce a color change with the Biuret reagent. However, when amino acids are part of a polypeptide or protein, they will react positively with the Biuret test.
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.
Will methionine give lead acetate test?
Lead acetate test is used to detect the presence of sulfur-containing amino acids like cysteine and homocysteine, not methionine. Methionine does not give a positive result in the lead acetate test.
What element in the amino acid is detected to be present in the lead acetate test?
The element that is detected in the lead acetate test for amino acids is sulfur. This test is used to identify the presence of sulfhydryl (thiol) groups in amino acids, which react with lead acetate to form a precipitate.
Do branch chain amino acids show up on a drug test?
no
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.
Why does Biurets reagent react with proteins but not amino acids?
Biurets reagent reacts with proteins because proteins contain multiple peptide bonds between amino acids, resulting in the formation of a violet color complex. Amino acids, on the other hand, do not have enough peptide bonds to form the complex with Biurets reagent.
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.
