In this study,the degradation of
neurofilament protein and modification on erythrocyte spectrin was demonstrated
in CS 2 treated rats at an exposure level of 1 200,2 400mg/m 3 by inhalation for two months.Spinal cords were removed from both CS 2 treated and non treated rats and NF riched cytoskeletal protein from spinal cords was prepared.A singnificant decrease was found in two subunit(200 and 70KDa)of
neurofilament by quantitative assessment of cytoskeletal protein using Dual wavelength TLC scanner.The
erythrocytic membrane was separated by ultra centri fugation.Covalent crosslinking of erythrocyte spectin was determined by SDS PAGE and TLC scanner.An abnormal high molecular weight band was found in CS 2 treated animals and a dose effect relationship was observed between the content of abnormal structure and CS 2 exposure level.It is suggested that the covalent cross linking of proteins has been considered as a potential mechanism for toxicity of carbon disulfide.