Development and characterization of human and mouse specific antibodies toCuZn-superoxide dismutase (SOD1)

Mutations in the copper/zinc superoxide dismutase (SOD1) gene are associate d with 15-20% of the familial forms of motor neuron disease. Mice where a t ransgene has been incorporated that encodes for the human SOD1 mutation dev elop a form of motor neurone disease that closely resembles human forms of this disease. We have produced and characterized species-specific antibodie s to epitopes in the SOD1 protein, amino acids 25-37, a region that disting uishes between the human and the mouse species of SOD1. The antisera genera ted were unable to immunoprecipitate the mouse or the human forms of SOD1 f rom tissue extracts unless the homodimeric complex of SOD1 was denatured. A s SOD1 exists as a homodimeric complex in the cytoplasm of cells, this sugg ests that amino acids in position, 25-37 are close to the dimeric interface of SOD1. (C) 2000 Elsevier Science B.V. All rights reserved.