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Antigenic analysis of the major human phosphoglucomutase isozymes:PGM1, PGM2, PGM3 and PGM4
Author(s) -
Drago G. A.,
Hopkinson D. A.,
Westwood S. A.,
Whitehouse D. B.
Publication year - 1991
Publication title -
annals of human genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 77
eISSN - 1469-1809
pISSN - 0003-4800
DOI - 10.1111/j.1469-1809.1991.tb00852.x
Subject(s) - phosphoglucomutase , isozyme , biology , polyclonal antibodies , antiserum , locus (genetics) , isoelectric focusing , biochemistry , genetics , microbiology and biotechnology , antigen , enzyme , gene
Summary The cross‐reactivity of human phosphoglucomutase isozymes (PGMl, PGM2, PGMS and PGM4) has been investigated using anti‐rabbit muscle PGM polyclonal antibodies. Significant differepces were revealed: an IgG fraction of the antiserum reacted with the primary and secondary PGMl isozymes of all the common phenotypes. However, there was no reaction with the PGM2 or PGM3 isozymes; thus these latter isozymes share no major antigenic determinants with human or rabbit PGMl and are therefore structurally distinct. In contrast, the PGM isozymes of human milk attributed to a fourth locus, PGM4, showed similar cross‐reactivity as PGMl suggesting close structural similarity. The IgG was also employed as a'reagent to remove PGMl from haemolysates so as to allow the unambiguous assessment of the PGMS isozyme patterns by isoelectric focusing. However, no proven genetic variation was encountered in a sample of 32 individuals.