A. Abrams, C. Baron
Nov 25, 1970
Citations
0
Influential Citations
39
Citations
Journal
Biochemical and biophysical research communications
Abstract
Abstract Dicyclohexylcarbodiimide (DCCD) inhibits the membrane ATPase of Streptococcus fecalis indirectly through a reaction with another membrane component as yet unidentified. Whether or not DCCD reacts covalenly to produce this inhibition is also not known. We have now found that several other carbodiimide compounds differing greatly from DCCD in structure and water solubility are also inhibitory. However, the hydrophobic carbodiimides were more potent by many orders of magnitude. Since structurally diverse carbodiimides could inhibit the membrane-bound ATPase we conclude that the inhibition results from a covalent reaction. The relatively high potency of the hydrophobic carbodiimides indicates that the reactive site is located within a non-polar region of the membrane. It is suggested that hydrophobic carbodiimides such as DCCD, by partitioning in the lipid phase of the membrane can reach a local concentration sufficiently high to react covalently with a membrane protein functional group.