INTERACTION OF DODECYL AND TETRADECYL SULFATE WITH PROTEINS DURING POLYACRYLAMIDE-GEL ELECTROPHORESIS

被引：20

作者：

DOHNAL, JC ^{[1
]}

GARVIN, JE ^{[1
]}

机构：

[1] NORTHWESTERN UNIV,SCH MED,DEPT BIOCHEM,CHICAGO,IL 60611

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 576卷 / 02期

关键词：

Dodecyl sulfate; Glycophorin; Protein-detergent binding; SDS polyacrylamide gel electrophoresis; Tetradecyl sulfate;

D O I：

10.1016/0005-2795(79)90414-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

1. 1. The affinity of tetradecyl sulfate for many unfolded proteins is greater than that of dodecyl sulfate. 2. 2. It is the presence of tetradecyl sulfate that results in the staining of proteins by pinacryptol yellow seen by Stoklosa and Latz (Stoklosa, J.T. and Latz, H.W. (1974) Biochem. Biophys. Res. Commun. 58, 74-79), as some tetradecyl sulfate remains associated with proteins during electrophoresis at room temperature (as opposed to dodecyl sulfate which, within the limit of detection, is completely removed). 3. 3. Tetradecyl sulfate has a greater capacity to dissociate protein aggregates which consist of identical peptide chains, such as Glycophorin dimers and bovine serum albumin dimers, than does dodecyl sulfate. © 1979.

引用

页码：393 / 403

页数：11

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