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α‐Galactosidase isozymes in normal individuals, and in Fabry hemizygotes and heterozygotes
Author(s) -
SØRENSEN S. A.,
HASHOLT LIS
Publication year - 1980
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.1469-1809.1980.tb01565.x
Subject(s) - isozyme , heterozygote advantage , locus (genetics) , isoelectric focusing , microbiology and biotechnology , staining , biology , biochemistry , neuraminidase , chemistry , allele , enzyme , genetics , gene
Summary A method for staining of α‐galactosidase with the synthetic substrate a‐naphthyl‐α‐galacto‐pyranoside after isoelectric focusing on gel slabs has been devised. Depending on the method used for cell extraction, at least seven isozymes could be detected in cell extracts of cultured fibroblasts from normal individuals. Thermal treatment revealed that both heat‐stable and heat‐labile isozymes occur in normal fibroblasts. The heat‐IabiIe isozymes were not detected in cells from Fabry hemizygotes and thus truly reflect products of the a‐gal A locus. Three heat‐stable isozymes observed in normal individuals were also found in Fabry heterozygotes and hemizygotes and are presumably determined by the α‐gal B locus. The remaining isozymes were stained very weakly in the hemi‐zygotes and were heat‐stable. The relation of these isozymes to the A or B locus is uncertain. After treatment with neuraminidase the =I‐gal A isozymes could not be detected and one of the α‐gal B isozymes appeared broader. The isozyme pattern observed in heterozygotes was almost identical to the normal one.