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

Why is hydrolysis of sucrose also known as specific sucrose test?

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?

The 3 proteins have the following properties. Which is the correct order of steps to extract them? + ethyl acetate, + (NH4)2SO4 at 20% saturation, centrifugation, + detergent (Triton X), buffer the lysate (pH=10), centrifugation, collect precipitate + ethyl acetate, + detergent (Triton X), + (NH4)2SO4 at 20% saturation, centrifugation, buffer the lysate (pH=10), centrifugation, collect precipitate + 1 M NaCl, + detergent (sodium dodecyI suIfate), centrifugation, +(NH4)2SO4 at 60% saturation, buffer at pH 7, centrifugation, collect precipitate + ethyl acetate, adjust pH to 7.3, centrifugation, collect supernate, +detergent (Triton X) to precipitate, +(NH4)2SO4 at 30% saturation, centrifugation, collect precipitate

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

Laemmli buffer, also referred to as SDS-reducing buffer, is added to each of the samples. It is a blue solution and the recipe for 2X Laemmli buffer is: 0.125 M Tris HCl, pH 6.8, 20% glycerol, 4% SDS and 10% β-mercaptoethanol (βME). What is the purpose of each of these ingredients?

A mixture of dipeptides consisting of Lys-Gly, Thr-His, Ser-Leu, Glu-Gln was applied to column packed with cation-exchange resin at pH 6.0. Which of these dipeptides would be eluted from the column first? O Lys-Gly first O Thr-His first O Ser-Leu first O Glu-Gln first OA mixture of Thr-His and Ser-Leu first

Consider a crude extract with a mixture of the 5 proteins listed below. Protein A 4.5 pl 160 molecular weight, kDa Protein B 12.5 pl and 65 molecular weight Protein C 5.0 pl, 15 molecular weight Protein D 6.8 pl, 150 molecular weight Protein E 9.5 pl, 45 molecular weight You load this protein mixture onto an anion exchange column at pH 11. Next, you apply a "washing" step by passing through buffer at pH 11. Finally, for your elution step, you apply a pH gradient starting from pH 11 to pH 2.0 (A gradient buffer system allows you to gradually and continuously change the pH of your mobile phase starting from pH 11 up to pH 2). You load this same protein mixture onto a Size Exclusion column. Please indicate the order in which these proteins will elute for both. Group of answer choices Yes or No, please explain your answer. If your protein of interest is protein A, would using anion exchange column be completely successful at separating it from all the other proteins? Group of answer…

If I had a standard with 2.0 mL of Bradford reagent then added 50μL of 250 μL/mL ; what would be the concentration of original protein?