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Decreased thermal stability of red blood cellglu 100 →gly superoxide dismutase from a family with amyotrophic lateral sclerosis
Author(s) -
Christine C. Winterbourn,
Neil M. Domigan,
Jennifer Broom
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00708-h
Subject(s) - amyotrophic lateral sclerosis , superoxide dismutase , mutant , polyacrylamide gel electrophoresis , chemistry , biochemistry , dismutase , enzyme , gel electrophoresis , microbiology and biotechnology , biology , medicine , gene , disease
Familial amyotrophic lateral sclerosis is a degenerative motor neuron disease associated in some cases with the presence of a mutant form of Cu/Zn superoxide dismutase. We have studied the stability of thegly 100 →glu mutant in extracts of red cells obtained from members of a family with a history of the disease. Extracts containing the mutant had an average 68% of normal superoxide dismutase activity. On heating at 65°C, these extracts lost activity at twice the rate of extracts containing only the normal enzyme. Decreased heat stability was also evident on native polyacrylamide gel electrophoresis with activity staining. This showed selective loss of first the mutant homodimer and then the heterodimer of the enzyme. Decreased stability intracellularly could be a factor in motor neuron degeneration.