Detail of "35888-63-2"

Reference

Kinetic analysis of the inhibition of sulfate transport in human red blood cells by isothiocyanates

Kinetic analysis of the inhibition of sulfate transport in human red blood cells by isothiocyanates. Rakitzis, Emmanuel T.; Gilligan, Paul J.; Hoffman, Joseph F. (Dep. Physiol., Yale Univ. Sch. Med., New Haven, Conn., USA). J. Membr. Biol., 41(2), 101-15 (English) 1978. CODEN: JMBBBO. ISSN: 0022-2631. DOCUMENT TYPE: Journal CA Section: 3 (Biochemical Interactions) A kinetic anal. of anion self-exchange in human red blood cells, in the presence of an irreversible inhibitor, is presented and applied to the study of the inactivation of sulfate transport by 3 isothiocyanates: disodium 3-isothiocyano-1,5-naphthalenedisulfonate (INDS) [35888-63-2], sodium 1-isothiocyano-4-naphthalenesulfonate (INS) [19182-24-2], and sodium 1-isothiocyano-4-benzenesulfonate (IBS) [17614-69-6]. The time dependence of the inhibition of sulfate transport by the isothiocyanates could be described by a single exponential, and contained a reversible and an irreversible component. In each case a portion of sulfate efflux was resistant to inactivation. The residual portion of the sulfate efflux varied with inhibitor: 4% for INS, 16% for INDS, and 34% for IBS. INS showed the largest reversible inhibitory effect, and INDS showed the weakest effect. IBS had the highest rate of inactivation and INDS the lowest. All 3 isothiocyanates apparently bind reversibly to an inhibitory site on the membrane before they bind covalently, and therefore irreversibly, to the same site on the membrane. The equil. const. for the dissocn. of the reversibly-bound complex and the rate of irreversible inactivation after all membrane sites are reversibly bound were computed for all 3 inhibitors.