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Isolation and characterization of heat-stable allergens from shrimp (Penaeus indicus)

Nagpal, Sunil and Rajappa, Lekha and Metcalfe, Dean D and Rao, Pillarisetti Subba V (1989) Isolation and characterization of heat-stable allergens from shrimp (Penaeus indicus). In: Journal of Allergy and Clinical Immunology, 83 (1). pp. 26-36.

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Official URL: http://dx.doi.org/10.1016/0091-6749(89)90474-0

Abstract

Shrimp are among the more common causes of immediate hypersensitivity reactions to food. To characterize better the allergenic substances within shrimp, extracts from heated shrimp were systematically examined with solid-phase radioimmunoassay and sera from patients clinically sensitive to shrimp. Two heat-stable protein allergens, designated as Sa-I and Sa-II, were identified from boiled shrimp (Penaeus indicus) extracts. Sa-I was isolated by ultrafiltration, Sephadex G-25, and diethylaminoethyl-Sephacel chromatography, whereas Sa-II, the major allergen, was purified by successive chromatography on diethylaminoethyl-Sephacel, Bio-Gel P-200, and Sepharose 4B columns. Sa-I, which was homogeneous by polyacrylamide gel electrophoresis (PAGE), elicited a single band on sodium dodecyl sulfate-PAGE corresponding to a molecular weight of 8.2 kd. Sa-II was also found to be homogeneous by PAGE, crossed immunoelectrophoresis, and immunoblotting. On sodium dodecyl sulfate-PAGE, it elicited a single band with a molecular weight of 34 kd. Sa-II was found to contain 301 amino acid residues and was particularly rich in glutamate/glutamine and aspartate/asparagine. Solid-phase radioimmunoassay-inhibition studies revealed that Sa-I and Sa-II share 54% of the allergenic epitopes, suggesting that Sa-I may be a fragment of Sa-II.SDS-PAGE, Sodium dodecyl sulfate-polyacrylamide gel electrophoresis; MW, Molecular weight; BSA, Bovine serum albumin; DEAE, Diethylaminoethyl; SPRIA, Solid-phase radioimmunoassay; CIE, Crossed immunoelectrophoresis .

Item Type: Journal Article
Publication: Journal of Allergy and Clinical Immunology
Publisher: Elsevier science
Additional Information: Copyright of this article belongs to Elsevier science.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 14 Oct 2010 08:26
Last Modified: 14 Oct 2010 08:26
URI: http://eprints.iisc.ac.in/id/eprint/33188

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