ovalbumin and dodecyl-sulfate

The sodium salts of representatives of anionic surfactants, dodecylbenzene sulfonate (SDBS), dodecyl sulfate (SDS) and coconut oil fatty acids, and a nonionic surfactant, dodecyl alcohol ethoxylate, were studied for adjuvant effect on the production of specific IgE antibodies in mice. The surfactants were injected subcutaneously (sc) in concentrations of 1000, 100, 10 or 1 mg/l, respectively, together with 1 microg of ovalbumin (OVA). In addition, groups of mice received OVA in saline (control group) or in Al(OH)(3) (positive adjuvant control group). After the primary immunization the mice were boosted up to three times with OVA (0.1 microg sc) in saline. OVA-specific IgE antibodies were determined by the heterologous mouse rat passive cutaneous anaphylaxis test. The results were confirmed by a specific ELISA method. After the first booster, the Al(OH)(3) group and the 10 mg/l SDS group showed a statistically significant increase in OVA specific IgE levels. After two boosters, a statistically significant suppression in OVA-specific IgE production occurred with SDS (1000 mg/l), SDBS (1000 and 100 mg/l), coconut soap (1000 mg/l) and the alcohol ethoxylate (10 mg/l). This study suggests that a limited number of surfactants possess an adjuvant effect whereas all surfactants at certain levels can suppress specific IgE production.

Topics: Adjuvants, Immunologic; Animals; Animals, Outbred Strains; Benzene Derivatives; Coconut Oil; Enzyme-Linked Immunosorbent Assay; Female; Immunoglobulin G; Injections, Subcutaneous; Male; Mice; Mice, Inbred BALB C; Ovalbumin; Plant Oils; Polyethylene Glycols; Rats; Rats, Sprague-Dawley; Sodium Dodecyl Sulfate; Surface-Active Agents

We describe the construction and use of a dodecyl sulfate-sensitive electrode cell to measure the activity of the detergent in biological samples. The electrode is based on the incorporation of a cetyltrimethylammonium/dodecyl sulfate complex in a siloxane polymer membrane. The cell records changes in the activity of SDS from 10(-6) to 10(-5) M SDS up to the critical micellar concentration. In aqueous solutions the cell follows Nernst' law with an electrometric response which is not affected by protein per se, but is modified by supporting electrolytes like NaCl. We demonstrate by comparison with equilibrium dialysis that the electrode can be used both to detect the high-affinity binding sites of serum albumin for SDS and to follow cooperative binding of the detergent to serum albumin, ovalbumin, and beta-lactoglobulin in the concentration interval 10(-4)-10(-3) M of unbound SDS. We conclude that the electrode has properties which should enable its use to monitor changes in SDS activity during interaction with biological material. The electrode may also be used to measure the activity of other detergents which, like SDS, form a sparingly soluble complex with cetyltrimethylammonium bromide.

Topics: Calibration; Detergents; Electrodes; Humans; Lactoglobulins; Ovalbumin; Protein Binding; Serum Albumin; Sodium Dodecyl Sulfate; Solubility; Water