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A novel catalase mutation detected by polymerase chain reaction‐single strand conformation polymorphism, nucleotide sequencing, and Western blot analyses is responsible for the type C of Hungarian acatalasemia
Author(s) -
Góth László,
Rass Péter,
Madarasi Irén
Publication year - 2001
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200101)22:1<49::aid-elps49>3.0.co;2-w
Subject(s) - microbiology and biotechnology , polymerase chain reaction , single strand conformation polymorphism , biology , exon , genetics , polymerase , primer (cosmetics) , intron , gene , southern blot , mutation , nucleic acid sequence , chemistry , organic chemistry
Polymerase chain reaction‐single strand conformation polymorphism (PCR‐SSCP) screening was used for searching mutations of the catalase gene in two Hungarian hypocatalasemic families. A syndrome‐causing mutation was found in a PCR product containing exon 7 and its boundaries. Nucleotide sequence analyses detected a G to T substitution at position 5 of intron 7. The effect of this splice site mutation was confirmed by Western blot analyses demonstrating a decreased catalase protein level in these patients. These findings represent a novel type (C) of catalase mutations in the Hungarian acatalasemic/hypocatalasemic patients.