Hybrid, immobilised dimers of human liver arginase.
The activity of matrix-bound monomers of arginase (L-arginine amidinohydrolase, EC 3.5.3.1) was not changed by incubation with p-hydroxymercuribenzoate. When the chemically modified, matrix-bound monomers were incubated with soluble subunits in the presence of Mn2+, dimers were obtained. These dimers were hybrids between modified and native monomers. The results obtained are in accord with a D2-symmetry where two dimers meet to form the tetrameric enzyme. From kinetic studies it is concluded that the structure of the active sites of arginase is not affected by the chemical modification with p-hydroxymercuribenzoate.
D001119:Arginase / Q000378:metabolism*; D001665:Binding Sites / Q000187:drug effects; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006801:Humans; D006902:Hydroxymercuribenzoates / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D008345:Manganese / Q000494:pharmacology
D004800:Enzymes, Immobilized; D006902:Hydroxymercuribenzoates; D046911:Macromolecular Substances; D008345:Manganese; D001119:Arginase