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The estimation of red cell superoxide dismutase activity by pulse radiolysis in normal and trisomic 21 subjects
Author(s) -
Gilles L.
Publication year - 1976
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(76)80652-7
Subject(s) - art , philosophy , humanities , physics
In Down’s syndrome, resulting from an abnormality of chromosome number, trisomy 21 [ 11, it is assumed that the extra-chromosome is the direct cause of the described morphological and biochemical changes. Numerous reports have appeared describing various enzymatic changes in such patients, but the mechanism by which they are produced as well as the localisation of the structural gene on chromosome 21 are unknown. However a direct relationship between chromosome 21 number and the amount of enzyme is the simplest hypothesis. Since the gene for cytosol superoxide dismutase (SODi) has been assigned to chromosome 21 using mouse-human somatic cell hybrids [2], it was interesting to study this enzyme in Down’s syndrome. The use of indirect assay systems [3,4] as well as immunological estimations [5], strongly suggested a proportional increase in the amount of synthesized enzyme. So we proposed to develop a direct assay method of erythrocyte superoxide dismutase using pulse radiolysis. Cytosol superoxide dismutase has been isolated from a wide range of cells including human erythrocytes and has been finally identified as erythrocuprein, the erythrocyte copper-containing protein [6,7]. This enzyme catalyses the reaction: