Sample 1 front contains 5,000 of methyl n-amyl ketone and the back section contains 200 µg of methyl n-amyl ketone Sample 2 front contains 4,000 µg of methyl n-amyl ketone and the back section contains 50 µg of methyl n-amyl ketone

This test will differentiate between aromatic amino acids with an acitivated ring from other amino acids. a) Nihydrin Test b) Xanthoproteic Test C) solubility test d) polarimeter test

Example of a Protein Purification Scheme: Purification of the Enzyme Xanthine Dehydrogenase from a Fungus Volume Total Total Specific Percent Fraction (mL) Protein (mg) Activity Activity Recovery 1. Crude extract 2. Salt precipitate 3. Ion-exchange chromatography |4. Molecular-sieve chromatography 5. Immunoaffinity chromatography 3,800 22,800 2,460 0.108 100 165 2,800 1,190 0.425 48 65 100 720 7.2 29 40 14.5 23 1.8 275 152.108 11 Calculate the specific activity of step#4. Note that percent recovery=% Yield.

Complete the table below by adding (+) or (-) if eahc sample (amino acid or protein) below will test positive or negative, respectively.  sample  BIURET  NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOSKIN-COLE G                 W                 H                 Y                 C                 R                 HAIR                 GELATIN                 CASEIN                 PEPTONE                 Identify the amino acid that will give the following data: BIURET  NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOPSKIN-COLE - + + + - - + - Name of amino acid: structurte of the amino acid:

Does all reducing sugars give a positive result in the Osazone test?

Using 25 µl of a patient's serum, how much diluent would be needed to create a 1:2 dilution?

Please answer and explain this Biochemsitry Question to the best of your ability

Consider the proteins in the table below. Protein Isoelectric point (pl) М.W. Alcohol dehydrogenase 150,000 5.5 Cytochrome C 12,400 10.5 Serum albumin 66,000 5.3 B-Amylase 200,000 5.7 Apoferitin 443,000 4.0 Fill in the blank. If the mixture of proteins above was subjected to anion exchange chromatography at pH 8, from the column. would be the first protein to elute

Order the steps of the Edman degradation. Not all the steps are used. extract the derivatized amino acid First Last Answer Bank treat with trifluoroacetic acid identify the phenylthiohydantoin treat with 6 M HCI treat with dinitrofluorobenzene treat with phenyl isothiocyanate

After doing the preliminary studies on redcrest protein extract, Tighnari proceeded with its characterization and analysis proper. He purified the crude protein extract through ammonium sulfate precipitation (40-60%) and gel filtration chromatography. Shown below are the results of the analyses. ||||| 250 kDa Crude Protein Extract 200 kDa 100 kDa 80 kDa 40 kDa 20 kDa ||| || Partially Purified Protein Extract Purified Protein Extract Figure D.1. Electrophoretogram obtained after NATIVE PAGE of the provided protein extracts. PAGE Analysis: 1. Based on Figure D.1., the series of purification procedures led to the isolation of two major redcrest proteins, COL and LEI. Determine the molecular weight of COL and LEI if the results of GFC showed that COL eluted out of the column first.