Immunological studies on erythrocyte phosphoglucomutase isozymes.
Human erythrocytes (phenotype PGM1 a1 or PGM1 a3) contain two sets of phosphoglucomutase isozymes, produced by the expression of the PGM1 and and PGM2 loci. The two sets are constituted each by two forms, of which that called "secondary" is thought to derive from the post-translational modification of that called "primary". Cross-reactivities of these isozymes were studied by means of monospecific rabbit antibodies against purified human red cell PGM1 and PGM2 "primary" isozymes. The results show that the PGM1 and PGM2 forms are not immunologically related and provide further proof of the post-synthetic origin of "secondary" isozymes and of the multifunctionality of PGM2 phosphoglucomutases.
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Istituto di Chimica Biologica Giorgio Fornaini, Università degli Studi di Urbino, Italy.
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D000906:Antibodies / Q000276:immunology / Q000494:pharmacology; D000918:Antibody Specificity; D000941:Antigens / Q000276:immunology; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D005779:Immunodiffusion; D007527:Isoenzymes / Q000097:blood* / Q000276:immunology; D010733:Phosphoglucomutase / Q000097:blood* / Q000276:immunology
D000906:Antibodies; D000941:Antigens; D007527:Isoenzymes; D010733:Phosphoglucomutase