Discussion: Commented [pa1]: .

First, it provides a place where the data

In the experiment, it was concluded that the unknown protein was BSA. The 6th band was the
thickest one, which it was indicated that the unknown protein was lying on that band. With the
use of the BlueStar Plus Prestained Protein Marker, it was found that the BSA was a molecular
weight of 66,5 kDa, the value closer to the molecular weight found in the experiment. The
molecular weight that the unknown protein was 63 kDa.
BSA is s a serum albumin protein derived from cows and it is used in the lab experiments due
to its protein concentration. It helps with the stabilization of the restriction enzymes during the
digestion of DNA.
may be fully discussed and interpreted, and second, it allows
the author to delve into the realms of speculation. Here one
may address questions like "why did something unexpected
happen?"; "what would happen if the reaction were carried
out at higher pH?"; "why did the expected results not
materialize?"
Commented [pa2]: 1.Identification of the unknown
protein based on the molecular weight
2.Identification of the low and high concentration
between Y and Z.

In this experiment, we used the method of SDS-PAGE for the purpose of protein separation.
You observe the movement of the charged molecules in an electric field with the support of a
medium, which in this experiment, we used a polyacrylamide gel. The polyacrylamide gel that
was used in the experiment is synthetic, thermo-stable, transparent, strong and chemically
unreactive. The pore size of the gel can be determined by the amount of acrylamide used. This
experiment is used to find out the protein size, protein identification, the sample purity,
identification of disulfide bonds, blotting applications and quantification of the protein.
During the migration, the smaller protein will migrate faster due to their molecular weight and
due to the less resistance, that exist. Moreover, expect from the resistance and the molecular
weight of the protein, the structure and the charge of the proteins play a role in the migration.
Due to the use of the sodium dodecyl sulfate and the polyacrylamide gel, the structure and the
charge of the protein do not influence the migration, and thus the proteins are separated only
based on the polypeptide chain length. SDS also gives all proteins the same linear, unfolded
structure and charge to weight ratio.

It also found that Y protein had a higher concentration with a molecular weight of 53 kDa,
while the Z protein had a lower concentration with a molecular weight of 57 kDa. The 6th bands
were the thickest in both ladders. Commented [pa3]: Not sure about it.

CEP57 is the protein with the molecular weight of 75 kDa. Commented [pa4]: Not sure about it.