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Binding of Lithium Dodecyl Sulfate to Polyacrylamide Gel at 4 Degrees C Perturbs Electrophoresis of Proteins

Binding of Lithium Dodecyl Sulfate to Polyacrylamide Gel at 4 Degrees C Perturbs Electrophoresis of Proteins

K Kubo, T Takagi

Anal Biochem. 1986 Jul;156(1):11-6.

PMID: 3740404

Abstract:

Although polyacrylamide gel has no affinity to lithium dodecyl sulfate (LDS) at 25 degrees C, the gel maximally binds 17 mg of LDS per gram dry weight at 4 degrees C. When polyacrylamide gel electrophoresis is carried out at 4 degrees C in the presence of LDS instead of sodium dodecyl sulfate (SDS) using a continuous buffer system, migration of proteins with lower molecular weight is accelerated as a result of the deficiency of LDS in the frontal region of the gel. When the gel is saturated with LDS, electrophoresis in the presence of LDS at 4 degrees C shows a resolution higher than that of SDS-polyacrylamide gel electrophoresis at 25 degrees C.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP2044566	Lithium dodecyl sulfate		2044-56-6	Price

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