Binding of [1-14C]methyl isocyanate to erythrocyte membrane proteins.
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.
Bhattacharya
B K
BK
Department of Biochemistry, Defence Research and Development Establishment, Gwalior, India.
Sharma
S K
SK
Jaiswal
D K
DK
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
D001457:Anion Exchange Protein 1, Erythrocyte; D002250:Carbon Radioisotopes; D017953:Isocyanates; D008565:Membrane Proteins; C008461:methyl isocyanate