Reference

Synergic effect on in vitro surface IgE synthesis of purified allergen and Sepharose-Con A

Synergic effect on in vitro surface IgE synthesis of purified allergen and Sepharose-Con A. Cocchiara, Roberta; Amoroso, Saverio; Geraci, Domenico (Ist. Biol. Sviluppo, Palermo, Italy). Monogr. Allergy, 18(Prog. Clin. Immunol.), 238-41 (English) 1983. CODEN: MOALAR. ISSN: 0077-0760. 11028-71-0 and 9012-36-6 which are cas registry numbers of chemicals are mentioned. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) Surface IgE formation in vitro, by IgE-bearing mononuclear cells (MNC) (isolated from humans), could be detected directly in a microculture system without any manipulation by using an ELISA. The synthesis of surface IgE was modulated by Sepharose-Con A and allergen mols. (pollen). Simultaneous stimulation by the 2 agents resulted in an synergistic enhancement of IgE formation in the MNC from atopic, as compared to normal humans. .

Isoelectric focusing of human IgA and secretory proteins using thin layer agarose gels and nitrocellulose capillary blotting

Isoelectric focusing of human IgA and secretory proteins using thin layer agarose gels and nitrocellulose capillary blotting. Elkon, K. B. (Div. Rheum. Dis., Hosp. Spec. 9012-36-6 and 9041-92-3 are cas registry numbers. These chemicals are also mentioned in this article. Surg., New York, NY, USA). J. Immunol. Methods, 66(2), 313-21 (English) 1984. CODEN: JIMMBG. ISSN: 0022-1759. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) A simple, rapid and economical method for focusing human IgA in low electroendosmosis agarose is described. IgA prepns. isolated from serum and secretions were focused with high resoln. in thin layer gels. Serum and milk proteins were transferred to nitrocellulose sheets by capillary blotting and the spectrotype of total IgA detd. with radiolabeled anti-human IgA antibodies. The spectrotype of human IgA extended between the pH range 4.3-6.85. The spectrotypes of free secretory component and a-1 antitrypsin released from an IgA myeloma protein were detd. by a similar technique. These methods should prove useful in detg. the diversity of IgA antibodies whether or not the starting material is pure. .