A carboxy-terminal truncation of human α-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

Journal of Clinical Investigation

Volumn 98, Issue 8, 1996, Pages 1809-1817

  Miyamura, Nobuhiro ^a   Araki, Eiichi ^a   Matsuda, Kohji ^a   Yoshimura, Ryouhei ^a   Furukawa, Noboru ^a   Tsuruzoe, Kaku ^a   Shirotani, Tetsuya ^a   Kishikawa, Hideki ^a   Yamaguchi, Kohei ^b   Shichiri, Motoaki ^a  

^a KUMAMOTO UNIVERSITY   (Japan)

^b OITA PREFECTURAL HOSPITAL   (Japan)

Author keywords

de novo mutation; electroporation; one base insertion; site directed mutagenesis; X linked disorder

Indexed keywords

ALPHA GALACTOSIDASE; LYSOSOME ENZYME;

ALLELE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CASE REPORT; CONTROLLED STUDY; DELETION MUTANT; ENZYME ACTIVITY; ENZYME MODIFICATION; FABRY DISEASE; FEMALE; GALACTOSEMIA; HETEROZYGOTE; HUMAN; HUMAN CELL; LIPID METABOLISM; MONKEY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SITE DIRECTED MUTAGENESIS; X CHROMOSOME LINKED DISORDER;

EID: 10244224048     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI118981     Document Type: Article

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