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Identification and Purification of an External Antigenic Glycoprotein (Immobilization Antigen) From Pseudomicrothorax Dubius
Author(s) -
BOLIVAR IGNACIO
Publication year - 1980
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1980.tb04266.x
Subject(s) - glycoprotein , isoelectric focusing , antigen , concanavalin a , chromatography , sephadex , immunodiffusion , affinity chromatography , polyacrylamide gel electrophoresis , chemistry , sepharose , isoelectric point , biochemistry , biology , immunology , enzyme , in vitro
SYNOPSIS. A large, external glycoprotein with antigenic properties isolated from the ciliate Pseudomicrothorax dubius was found to have a molecular weight of ∼ 250,000 daltons. Analysis of the extracts by isoelectric focusing in combination with immunodiffusion and gradient polyacrylamide gel electrophoresis revealed that the principal antigen was a large glycoprotein. the glycoprotein was purified partially by Sephadex ultrafiltration. and almost completely by affinity chromatography on a concanavalin A‐Sepharose column.