PubMed:2152885 JSONTXT

{"project":"DisGeNET5_variant_disease","denotations":[{"id":"2152885-0#124#137#geners104894831","span":{"begin":124,"end":137},"obj":"geners104894831"},{"id":"2152885-0#10#25#diseaseC0002986","span":{"begin":10,"end":25},"obj":"diseaseC0002986"}],"relations":[{"id":"124#137#geners10489483110#25#diseaseC0002986","pred":"associated_with","subj":"2152885-0#124#137#geners104894831","obj":"2152885-0#10#25#diseaseC0002986"}],"text":"A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser.\nWe analyzed a male patient with Fabry's disease who had no activity of the lysosomal hydrolase alpha-galactosidase A (alpha-GalA) and female members of his family. We cloned a cDNA that encoded the mutant alpha-GalA, determined its nucleotide sequence, and found two nucleotide differences between the mutant and the wild-type cDNAs. Although one difference was silent, the other difference, a C-to-T transition at nucleotide number 118, resulted in an amino acid substitution of Pro-40 by Ser. A transient expression assay demonstrated that this missense mutation was the cause of the deficiency of alpha-GalA activity in the patient. In vitro mutagenesis experiments demonstrated that Pro-40 is critical for the appearance of alpha-GalA activity."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"2152885-0#47#68#gene2717","span":{"begin":47,"end":68},"obj":"gene2717"},{"id":"2152885-0#10#25#diseaseC0002986","span":{"begin":10,"end":25},"obj":"diseaseC0002986"}],"relations":[{"id":"47#68#gene271710#25#diseaseC0002986","pred":"associated_with","subj":"2152885-0#47#68#gene2717","obj":"2152885-0#10#25#diseaseC0002986"}],"text":"A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser.\nWe analyzed a male patient with Fabry's disease who had no activity of the lysosomal hydrolase alpha-galactosidase A (alpha-GalA) and female members of his family. We cloned a cDNA that encoded the mutant alpha-GalA, determined its nucleotide sequence, and found two nucleotide differences between the mutant and the wild-type cDNAs. Although one difference was silent, the other difference, a C-to-T transition at nucleotide number 118, resulted in an amino acid substitution of Pro-40 by Ser. A transient expression assay demonstrated that this missense mutation was the cause of the deficiency of alpha-GalA activity in the patient. In vitro mutagenesis experiments demonstrated that Pro-40 is critical for the appearance of alpha-GalA activity."}