Proteins are composed of amino acids. All amino acids are amphoteric molecules consisting of three types of amino acids: neutral, acidic, and basic. Thus, for any protein there is a characteristic pH, called the isoelectric point (pI), at which the protein has no net charge and therefore will not move in the electric field. Electrophoresis takes advantage of this characteristic. Proteins are electrophoreased, and the most negatively charged protein moves closest to the cathode, and the most positively charged protein moves closest to the anode. Cytochrome C was expected to move closest to the cathode, and serum albumin was expected to move closest to the anode. Only cytochrome C was expected to move to the cathode. The other three proteins were expected to move toward anode. The purpose of electrophoresis was to see how a difference in pI makes a difference in the electrophoretic mobility of protein.

Four proteins were electrophoreased by using the Tris-Glysin buffer of pH 8.6 and a horizontal agarose gel 1.1 % in isoelectric focusing (IEF) a

Ravnskov, U. (1975, February). Low molecular weight proteinuria in association with paroxysmal myoglobinuria. [Abstract] Clin Nephrol 1975 Feb;3(2). 65-9. Retrieved January 31, 2001 from the WWW: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=47277&dopt=Abstract

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