title: Binding of [1-14C]methyl isocyanate to erythrocyte membrane proteins.
abstract: We describe the interaction of methyl isocyanate with reactive sulphydryl groups of rat erythrocyte membrane proteins. Intraperitoneal administration, as well as in vitro incubation of methyl isocyanate, caused a significant reduction in the free sulphydryl content of erythrocyte membrane proteins. [1-14C]Methyl isocyanate was specifically bound to band III of the erythrocyte membrane and caused the breakdown of band III proteins.
authors.affiliation: Department of Biochemistry, Defence Research and Development Establishment, Gwalior, India.
authors.forename: B K
authors.initials: BK
authors.lastname: Bhattacharya
authors.forename: S K
authors.initials: SK
authors.lastname: Sharma
authors.forename: D K
authors.initials: DK
authors.lastname: Jaiswal
mesh_terms: D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000032:analysis; D002250:Carbon Radioisotopes; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism*; D005260:Female; D017953:Isocyanates / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D002250:Carbon Radioisotopes; D017953:Isocyanates; D008565:Membrane Proteins; C008461:methyl isocyanate