Compounds > 2-2--azino-di-(3-ethylbenzothiazoline)-6-sulfonic-acid

2-2--azino-di-(3-ethylbenzothiazoline)-6-sulfonic-acid and n-heptane

2-2--azino-di-(3-ethylbenzothiazoline)-6-sulfonic-acid has been researched along with n-heptane* in 1 studies

Other Studies

1 other study(ies) available for 2-2--azino-di-(3-ethylbenzothiazoline)-6-sulfonic-acid and n-heptane

Article	Year
Interaction of sodium bis(2-ethylhexyl) sulfosuccinate (AOT) with catalase and horseradish peroxidase in an aqueous solution and in the reverse micelles of AOT/N-heptane. Biochemistry and molecular biology international, 1998, Volume: 45, Issue:4 Some properties of catalase and horseradish peroxidase entrapped into reverse micelles of sodium bis(2-ethylhexyl) sulfosuccinate (AOT)/n-heptane with those in an aqueous solution of AOT are compared. Secondary structure of catalase significantly changes and activity is completely lost in the presence of aqueous micellar solution of AOT. In AOT/n-heptane reverse micelles secondary structure of catalase does not change. AOT has no effect on horseradish peroxidase in aqueous solution. On the other hand slight changes in secondary structure of horseradish peroxidase in AOT/n-heptane reverse micelles appear. It is concluded that electrostatic interactions between catalase or horseradish peroxidase with AOT molecule at neutral pH are not the main factor determining reactivity of investigated enzymes in reverse micelles. Topics: Benzothiazoles; Catalase; Circular Dichroism; Dioctyl Sulfosuccinic Acid; Heptanes; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Micelles; Oxidation-Reduction; Protein Structure, Secondary; Static Electricity; Sulfonic Acids	1998

Article

Year

Interaction of sodium bis(2-ethylhexyl) sulfosuccinate (AOT) with catalase and horseradish peroxidase in an aqueous solution and in the reverse micelles of AOT/N-heptane.

Biochemistry and molecular biology international, 1998, Volume: 45, Issue:4

Some properties of catalase and horseradish peroxidase entrapped into reverse micelles of sodium bis(2-ethylhexyl) sulfosuccinate (AOT)/n-heptane with those in an aqueous solution of AOT are compared. Secondary structure of catalase significantly changes and activity is completely lost in the presence of aqueous micellar solution of AOT. In AOT/n-heptane reverse micelles secondary structure of catalase does not change. AOT has no effect on horseradish peroxidase in aqueous solution. On the other hand slight changes in secondary structure of horseradish peroxidase in AOT/n-heptane reverse micelles appear. It is concluded that electrostatic interactions between catalase or horseradish peroxidase with AOT molecule at neutral pH are not the main factor determining reactivity of investigated enzymes in reverse micelles.

Topics: Benzothiazoles; Catalase; Circular Dichroism; Dioctyl Sulfosuccinic Acid; Heptanes; Horseradish Peroxidase; Hydrogen Peroxide; Hydrogen-Ion Concentration; Micelles; Oxidation-Reduction; Protein Structure, Secondary; Static Electricity; Sulfonic Acids

1998