Protein coloration reaction - a double-shrink reaction experiment.

and" protein" molecular structure contains many peptide bonds, the structure of which is the same as the paracetamol bonds in the dichotomy molecule. Therefore, under alkaline conditions, the color reaction with copper ions can also be similar to that of di-shrink. The reaction process is as follows:

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1. Protein solution (egg is diluted 10 times with distilled water, filtered out by 2-3 layers of sand cloth)

2.0.1% glycine solution

3. 0.01% arginine solution

4. 10% NaOH solution

5. 1% CuSO4 solution

6.urea crystallization

"experiment operation"

;"> takes a little urea crystallization (about the size of a matchhead) and puts"> dry" in"> test tubes", micro-fire heating to urea melt to harden, just hardened immediately stop heating, At this point, the double contraction is formed. After cooling, add 10% sodium hydroxide solution about 1 ml, and shock, and then add 1% copper sulfate solution 2 drops, and then shock, observe color changes.

Note:

a. Test tubes cannot be rushed to others during operation to prevent burns;

c. Heating can not be too large to prevent carbonization.

2. Observation phenomenon

1

2

3

4

protein sample liquid (ml)

1.0

0.01% arginine (ml)

1.0

0.1% glycine (ml)

2.0

2.0.

2.0

2.0

distilled water (ml)

1.0

.

phenomenon