Purification and characterization of a specific antigen from Echinococcus multilocularis.

Gottstein, Bruno (1985). Purification and characterization of a specific antigen from Echinococcus multilocularis. Parasite immunology, 7(3), pp. 201-212. Blackwell Scientific Publications

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A polypeptide (Em2a) purified by affinity chromatography from the Echinococcus multilocularis metacestode showed a high degree of purity as assayed by SDS-PAGE and analytical isoelectrical focusing. A minor contamination with host albumin was revealed. Estimation of relative mol. mass gave a value of 54,000. The isoelectric point was found to be 4.8. Antigenic activity of the polypeptide was demonstrated by immunoprecipitation and western blotting. In these assays the protein was recognized only by homologous sera from patients infected with larval E. multilocularis. This antigen (Em2a) did not react in the ELISA with sera from patients infected with heterologous helminths; these sera were highly cross-reacting with antigen from E. granulosus hydatid fluid. Seventy-three (94%) from 78 investigated patients (alveolar echinococcosis) showed a seropositive reaction with the polypeptide Em2a.

Item Type:

Journal Article (Original Article)

Division/Institute:

05 Veterinary Medicine > Department of Infectious Diseases and Pathobiology (DIP) > Institute of Parasitology
05 Veterinary Medicine > Department of Infectious Diseases and Pathobiology (DIP)

UniBE Contributor:

Gottstein, Bruno

Subjects:

600 Technology > 630 Agriculture

ISSN:

0141-9838

Publisher:

Blackwell Scientific Publications

Language:

English

Submitter:

Bruno Gottstein

Date Deposited:

21 Apr 2015 09:13

Last Modified:

21 Apr 2015 09:13

PubMed ID:

2409507

URI:

https://boris.unibe.ch/id/eprint/66742

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