Article
A carboxy-terminal truncation of human alpha-galactosidase A in a heterozygous female with Fabry disease and modification of the enzymatic activity by the carboxy-terminal domain. Increased, reduced, or absent enzyme activity depending on number of amino acid residues deleted.
The Journal of clinical investigation - 15 Oct 1996
Miyamura N, Araki E, Matsuda K, Yoshimura R, Furukawa N, Tsuruzoe K, Shirotani T, Kishikawa H, Yamaguchi K, Shichiri M
Abstract excerpt
Fabry disease is an X-linked disorder of glycosphingolipid metabolism caused by a deficiency of alpha-galactosidase A (alpha-Gal A). We identified a novel mutation of alpha-Gal A gene in a family with Fabry disease, which converted a tyrosine at codon 365 to a stop and resulted in a truncation of the carboxy (C) terminus by 65 amino acid (AA) residues. In a heterozygote of this family, although the mutant and...
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