A fluorescent method for the rapid staining and quantitation of proteins in sodium dodecyl sulfate‐polyacrylamide gels
- 1 January 1985
- journal article
- research article
- Published by Wiley in Electrophoresis
- Vol. 6 (11) , 527-531
- https://doi.org/10.1002/elps.1150061102
Abstract
Fluorescence studies carried out in solution indicate that in the presence of the anionic detergent sodium dodecyl sulfate (SDS) proteins are able to bind the noncovalent dye 1‐anilinonaphthalene‐8‐sulfonate (ANS). The interaction of this hydrophobic dye with protein‐SDS complexes is probably responsible for the fluorescence of protein bands observed by UV‐transillumination of polyacrylamide gels stained with ANS. It is shown that the staining of SDS‐polyacrylamide gels with ANS after electrophoresis allows the detection and quantitative estimation of proteins and peptides having different properties. The electrophoretic patterns obtained using ANS are equivalent to those obtained using Coomassie Brilliant Blue R‐250. The fluorescent staining method described in this work is simpler and much more rapid than conventional methods using visible dyes.This publication has 13 references indexed in Scilit:
- A fluorescent complex between ethidium bromide and nucleic acids: Physical—Chemical characterizationPublished by Elsevier ,2004
- Fluorescent properties of histone-1-anilinonaphthalene 8-sulfonate complexes in the presence of denaturant agents: Application to the rapid staining of histones in urea and Triton-urea-polyacrylamide gelsAnalytical Biochemistry, 1985
- Proteases as structural probes for chromatin: The domain structure of histonesBioscience Reports, 1984
- Rapid fluorescent staining of histones in sodium dodecyl sulfate-polyacrylamide gelsAnalytical Biochemistry, 1984
- [5] The role of micelles in protein—detergent interactionsPublished by Elsevier ,1979
- High-resolution preparative SDS-polyacrylamide gel electrophoresis: Fluorescent visualization and electrophoretic elution-concentration of protein bandsAnalytical Biochemistry, 1975
- Fluorometric scanning of fluorescamine-labeled proteins in polyacrylamide gelsAnalytical Biochemistry, 1974
- Fluorescence Probes for StructureAnnual Review of Biochemistry, 1972
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- A method for immediate visualization of proteins in acrylamide gels and its use for preparation of antibodies to enzymesAnalytical Biochemistry, 1969