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Name of Student: Saracho, Ezra Joseph G.

Date Performed: September 19, 2017


Group/ Section Number: Group 4/ 2L Date Finished: September 19, 2017

Exercise Number 4.4


Electrophoresis
A. Complete Data Blanks

Table 4.4. 1 Rf values of the protein standards and egg albumin sample
Protein MW (Daltons) Distance Distance Rf
Standards travelled by the travelled by the
sample (cm) tracking dye
(cm)
Phosphorylase 97000 1.4 3.9 0.36
B
Albumin 66000 2.2 3.9 0.56
Ovalbumin 45000 2.8 3.9 0.72
Carbonic 30000 3.4 3.9 0.87
anhydrase
Egg albumin sample
Ammonium 79602.32 1.8 3.7 0.49
sulfate 42541.51 2.8 3.7 0.76
precipitation
GFC pooled 85341.54 1.7 3.7 0.46
fractions
45608.70 2.7 3.7 0.73
1
0.87179
0.9
0.76 Protein
0.8 0.73
0.71735
Standards
0.7 Egg Albumin
0.6 0.5461
Rf Value

0.49 Linear (Protein


0.46
0.5 Standards)
0.35897
0.4
0.3
0.2
0.1
0
4.4 4.5 4.6 4.7 4.8 4.9 5 5.1
LOG MW

Figure 4.4. 1 Rf values of the protein standards and egg albumin sample
B. Discussion
There are multiple techniques for protein analysis. One of the most used technique
for identifying proteins. One of the most common is electrophoresis. It separates proteins
based on molecular size and charge. Electrophoresis uses a porous matrix to separate
proteins based on molecular size. It separates proteins by charges by using electricity
passed through the gel.
Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE) will be
the process used to separate and identify the proteins. The process only separates the
proteins by molecular size. The charge of the proteins is neglected by the anionic
detergent coating the proteins making the it a negatively charged rod.
The gel was already prepared beforehand so the process was only explained.
There are 2 gels needed to prepare the SDS PAGE gel, the stacking and separating
gel. The separating gel was first added to the cassette. The gel, as the name implies,
separates the proteins in a solution. The stacking gel on the other hand is where the
sample solutions are placed.
The samples to be tested are
C. References

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