Hopkins-Cole Test is used to detect the presence of tripthopahan.
The reagent contain glioksilic acid. Positive reaction will show purple color (ring) in the solution boundaries. The purple color occur by condensation of 2 core of tripthophan to glioksilic. This test can't succes if there are strong ocsidator like nitrat and clorat. Sulphuric acid that used must very pure, it is means that there aren't other matter which will be an ocsidator.
Procedure:
1. Take 2 ml of solution that will be tested in the test tube
2. Add with 2 ml of Hopkins-Cole reagent
3. Add H2SO4 from the wall of the test tube
4. Wait some seconds
5. See the color of solution.
Senin, 12 Maret 2012
Millon Test
Milon test is chemical reaction to detect the presence of tyrosine.
It is specific reaction to monophenol derivative as tyrosine. In this test we use mercury ion in the nitric acid. Positive test will show red color in the solution. The red color formed of salt from tyrosine nitration. Hidroxiphenil from tyrosine will react to Hg from millon reagent to produce red color.
Method to make millon reagent:
1. Take 2,5 gram of mercury sulphat and add with 5 ml HNO3
2. Add solution with 15 ml of aquadest
Procedure:
1. Take 2 ml of solution that will be tested in the test tube
2. Add the solution with 5 drops of millon reagent
3. White floe will seen, heated carefully
4. See the color of solution.
It is specific reaction to monophenol derivative as tyrosine. In this test we use mercury ion in the nitric acid. Positive test will show red color in the solution. The red color formed of salt from tyrosine nitration. Hidroxiphenil from tyrosine will react to Hg from millon reagent to produce red color.
Method to make millon reagent:
1. Take 2,5 gram of mercury sulphat and add with 5 ml HNO3
2. Add solution with 15 ml of aquadest
Procedure:
1. Take 2 ml of solution that will be tested in the test tube
2. Add the solution with 5 drops of millon reagent
3. White floe will seen, heated carefully
4. See the color of solution.
Sabtu, 10 Maret 2012
Xanthoproteic Test
Xanthoproteic test is used to detect the presence of tyrosine, phenilalanine, and tripthophane.
Benzene core in the amino acids above will be nitrated with HNO3 and forming nitro compound, the yellow color is formed and in the alchaly environment will change to orange color.
Important in this test is:
1. HNO3
2. NaOH
Procedure:
1. Take 2 ml of solution that will be tested in the test tube
2. Add 1 ml of HNO3
3. Look at the white pecipitate that formed
4. Boiled up ,the precipitate will dissappeared and will show yellow color of solution
5. Add NaOH drop per drop
6. The orange color will appear
Benzene core in the amino acids above will be nitrated with HNO3 and forming nitro compound, the yellow color is formed and in the alchaly environment will change to orange color.
Important in this test is:
1. HNO3
2. NaOH
Procedure:
1. Take 2 ml of solution that will be tested in the test tube
2. Add 1 ml of HNO3
3. Look at the white pecipitate that formed
4. Boiled up ,the precipitate will dissappeared and will show yellow color of solution
5. Add NaOH drop per drop
6. The orange color will appear
Ninhidrin Test
Ninhidrin test is chemical test to detect the presence of amino acids.
All kinds of amino acid can detected with this test. Amino acid reacted with ninhidrin (triketohidrindenhidrat) to forming aldehide and release Nh3 and CO2. In this reaction also formed blue color (but prolin and hidroxiprolin will show yellow color). The blue color is reaction of 2 molecule of ninhidrin with NH3. It is the signing of positive result for this test.
Procedure:
1. Take 2 ml of solution that will be tested to the test tube
2. Add with 5 drops of ninhidrin solutions
3. Boiled in 10 minutes
4. See the color of solution.
All kinds of amino acid can detected with this test. Amino acid reacted with ninhidrin (triketohidrindenhidrat) to forming aldehide and release Nh3 and CO2. In this reaction also formed blue color (but prolin and hidroxiprolin will show yellow color). The blue color is reaction of 2 molecule of ninhidrin with NH3. It is the signing of positive result for this test.
Procedure:
1. Take 2 ml of solution that will be tested to the test tube
2. Add with 5 drops of ninhidrin solutions
3. Boiled in 10 minutes
4. See the color of solution.
Biuret Test
Biuret test is chemical test to detect the presence of proteins, especially the presence of peptide bond.
Peptide bond is bonding each amino acids in the protein. Biuret can't detect the single amino acids, because there aren't peptide bond in it. Positive result will showing purple color, Cu++ will reacting with NH from peptide bond and O from water and show the purple color of solution. Long proteins show purple color, short proteins show pink color.
Important in this test is:
1. NaOH 10 %
2. CuSO4 0,1%
Procedure:
1. Take 2 ml of solution that will be tested to the test tube
2. Add with 2 ml of NaOH and 10 drops of CuSO4
3. See the color of solution.
Peptide bond is bonding each amino acids in the protein. Biuret can't detect the single amino acids, because there aren't peptide bond in it. Positive result will showing purple color, Cu++ will reacting with NH from peptide bond and O from water and show the purple color of solution. Long proteins show purple color, short proteins show pink color.
Important in this test is:
1. NaOH 10 %
2. CuSO4 0,1%
Procedure:
1. Take 2 ml of solution that will be tested to the test tube
2. Add with 2 ml of NaOH and 10 drops of CuSO4
3. See the color of solution.
Jumat, 09 Maret 2012
Protein Test
Proteins is polymer of amino acid which conected by peptide bond. There are 20 amino acids that arrange the proteins, the differ of protein has differ amino acids composition. Bellow you will see some test to detect proteins or certain amino acid.
1. Biuret test: to detect the presence of proteins, actually the presence of peptide bond
2. Ninhidrin test: to detect the presence of amino acids
3. Xanthoproteic test: to detect the presence of tyrosine, phenylalanine, and trypthophane
4. Milllon test: to detect the presence of tyrosine
5. Hopkins-Cole test: to detect the presence of trypthophan.
1. Biuret test: to detect the presence of proteins, actually the presence of peptide bond
2. Ninhidrin test: to detect the presence of amino acids
3. Xanthoproteic test: to detect the presence of tyrosine, phenylalanine, and trypthophane
4. Milllon test: to detect the presence of tyrosine
5. Hopkins-Cole test: to detect the presence of trypthophan.
Iodium Test
Iodium test/Lugol test is chemical test to detect the presence of amylum.
Amylum presence in many kinds of food, example: rices, corns, pottatoes, sweet pottatoes etc. The are two strains of amylum chains, they are: amylose ( long and straight chains ), amylopectine ( long and branched chains). Tested amylose with iodium will show blue color, but amylopectine will show purple color.
Procedure:
1. Take 3 drops of amylum solution and add 1 drop of iodium solution
2. See the color of solution
Amylum presence in many kinds of food, example: rices, corns, pottatoes, sweet pottatoes etc. The are two strains of amylum chains, they are: amylose ( long and straight chains ), amylopectine ( long and branched chains). Tested amylose with iodium will show blue color, but amylopectine will show purple color.
Procedure:
1. Take 3 drops of amylum solution and add 1 drop of iodium solution
2. See the color of solution
Langganan:
Postingan (Atom)