Serum Protein Electrophoresis (Spep)

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  • Topic: Proteins, Gamma globulin, Serum protein electrophoresis
  • Pages : 2 (310 words )
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  • Published : April 8, 2013
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Name: Fatma Al- Na'imat.
Reg. No. : 0105514.
Course: Immunology laboratory.
Instructor: Dr. Muna Hassuneh.
Report subject: Serum protein electrophoresis.
Report No.: 1.

Serum Protein Electrophoresis (SPEP)

Introduction:
The serum protein electrophoresis (SPEP) test measures specific proteins in the blood to help identify some diseases. And its uses an electrical field to separate the proteins in the blood serum into groups of similar size, shape, and charge. And here we'll use gel electrophoresis which indicate that blood serum is placed on special paper treated with agarose gel and exposed to an electric current to separate the serum protein components into five major fractions by size and electrical charge: serum albumin, alpha-1 globulins, alpha-2 globulins, beta globulins, and gamma globulins.

Results:
As shown in next page.

Discussion:
From what we observe in the gel results there are four bands and one smear, in seven lines which every line present a different serum (except 6 +7 are same 1 +2). Each band and the smear present different compound of serum protein. The first thick band is albumin which is the major fraction in a normal SPEP, and according to its concentration in serum it has the thicker band as its accounts for about 60 percent of the protein found in serum. Second band it’s a globulin protein it called Alpha-1 globulin it has the least concentration among the other globulins and albumin that’s explain the light color of its band. Third and forth bands are Alpha-2 globulin and Beta globulin respectively a close concentration values explain the bands thickness and color. The smear lastly is Gamma globulin although it has a close concentration as alpha 1 and beta globulin it has smeared zone and that’s due to its light molecular weight, so we conclude that another reason for the band thickness is the molecular weight of the proteins.
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