ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

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.

Full text not available from this repository.
Official URL: http://dx.doi.org/10.1016/0091-6749(89)90474-0


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
Related URLs:
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.ernet.in/id/eprint/33188

Actions (login required)

View Item View Item