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245	1	0	_aSDS polyacrylamide gel electrophoresis of proteins
490	0		_vIn Proteins. Humana Press, p.41-55 , 1984
520	3		_aProbably the most widely used of techniques for analyzing mixtures of proteins is SDS polyacrylamide gel electrophoresis. In this technique, proteins are reacted with the anionic detergent, sodium dodecylsulfate (SDS, or sodium lauryl sulfate)to form negatively charged complexes. The amount of SDS bound by a protein, and so the charge on the complex, is roughly proportional to its size. Commonly, about 1.4 g SDS is bound per 1 g protein, although there are exceptions to this rule. The proteins are generally denatured and solubilized by their binding of SDS, and the complex forms a prolate elipsoid or rod of a length roughly proportionate to the protein's molecular weight. Thus, proteins of either acidic or basic pI form negatively charged complexes that can be separated on the bases of differences in charges and sizes by electrophoresis through a sieve-like matr ix of polyacrylamide gel.
650	1	4	_aSODIUM LAURYL SULFATE
650	1	4	_aAMMONIUM PERSULFATE
650	1	4	_aACRYLAMIDE CONTENT
650	1	4	_aACRYLAMIDE MONOMER
650	1	4	_aRESERVOIR BUFFER
700	1	2	_aSmith, B. J.
856	4	0	_uhttps://drive.google.com/file/d/1j1t9b-IKX9axYf2B7-Xy-bmanPsuydpX/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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