Premium
Binding of [1‐ 14 C]Methyl Isocyanate to Erythrocyte Membrane Proteins
Author(s) -
Bhattacharya B. K.,
Sharma S. K.,
Jaiswal D. K.
Publication year - 1996
Publication title -
journal of applied toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.784
H-Index - 87
eISSN - 1099-1263
pISSN - 0260-437X
DOI - 10.1002/(sici)1099-1263(199603)16:2<137::aid-jat317>3.0.co;2-e
Subject(s) - isocyanate , band 3 , chemistry , membrane , erythrocyte membrane , incubation , in vitro , biochemistry , membrane protein , organic chemistry , polyurethane
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.