Human serum albumin is the most abundant protein in humanblood plasma. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin is essential for maintaining the osmotic pressure needed for proper distribution of body fluids between intravascular compartments and body tissues. It also acts as a plasma carrier by non-specifically binding several hydrophobicsteroid hormones and as a transport protein for hemin and fatty acids(1) In this paper, we decided to determine the structural kinetic stability of human serum albumin by different factors such as pH and temperature(2). How these factors affected the protein stability, were shown by IR spectrums. In acidic or alkaline environment, the number and type of hydrogen bands varied due to thevariation in OH-stretching and OH-bounding areas.Shift of the spectrum from 3400cm-1 to 4000cm-1 repreasents breakage of different strong and weak hydrogen bands and construction of concurrent new hydrogen bands. This events meant the obvious change in second structure of protein.In the area of 1800-2000cm-1, some changes happened. In the area of 1660cm-1 and 1584cm-1, the peaks were weakened and in 1730cm-1, the peak shifted in higher frequencies because of the variation in OH-bounding in intramolecular structure of water.In inert condition, we met no event.

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