Literature DB >> 6496933

Hydrogenation of triton X-100 eliminates its fluorescence and ultraviolet light absorption while preserving its detergent properties.

G E Tiller, T J Mueller, M E Dockter, W G Struve.   

Abstract

The ultraviolet-light absorption and fluorescence of Triton X-100 were virtually eliminated by hydrogenation to its reduced cyclohexyl analog, RTX-100. The critical micelle concentration of RTX-100 was 12% higher than that of Triton X-100. RTX-100 and Triton X-100 were quite similar in their abilities to extract proteins from human erythrocyte membranes.

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Year:  1984        PMID： 6496933     DOI： 10.1016/0003-2697(84)90455-x

Source DB:  PubMed          Journal:  Anal Biochem        ISSN： 0003-2697            Impact factor:   3.365


  14 in total

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2.  Mechanisms of Specific versus Nonspecific Interactions of Aggregation-Prone Inhibitors and Attenuators.

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3.  Carbohydrate-containing Triton X-100 analogues for membrane protein solubilization and stabilization.

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Journal:  Biochem J       Date:  1985-10-01       Impact factor: 3.857

5.  Adenine nucleotide translocase greatly increases the partition of trinitrophenyl-ATP into reduced Triton X-100 micelles.

Authors:  P J Tummino; A Gafni
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9.  Influence of cyclodextrin on the solubility and the polymerization of (meth)acrylated Triton(®) X-100.

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10.  Fluorophore Absorption Size Exclusion Chromatography (FA-SEC): An Alternative Method for High-Throughput Detergent Screening of Membrane Proteins.

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