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V Kalous

Publications and source records attributed to V Kalous.

7 recordsLinked to original sources
PubMed1975

Binding of D-glucose to insulin.

Binding of D-glucose to insulin has been studied by equilibrium dialysis. The binding is not very specific and probably takes place in two steps. The average amount of glucose molecules bound per insulin molecule is eight, two molecules in the first and six during the second step of binding. The intrinsic binding constants for both steps are almost the same (6-10-2 M-minus 1 and 1-10-3 M-minus 1) which can be explained by assuming: (1) that after binding of the first two molecules a conformational change of insulin occurs which facilitates the binding of the next six molecules of D-glucose; or (2) that in the second step of binding the glucose binds to hydrophobic regions which are unmasked by dissociation of the insulin dimer. Using a three-dimensional model of the insulin molecule areas of the protein molecule where binding of glucose can occur were selected. The glucose-binding site very probably involves the area at the insulin surface where most of the invariant and modification-selective residues are present.

Binding Sites↗
PubMedDate not supplied

On the mechanism of the insulin-glucose interactions.

Analysis of the course of D-glucose binding to insulin has shown that the mechanism of glucose-insulin interaction is a cooperative process. Binding of D-glucose molecules to insulin is facilitated by the dissociation of insulin aggregates caused by insulin-glucose interaction. Thus, insulin behaves as a system with strong positive cooperativity. The results have been treated in accordance with theories for interactions coupled to association equilibria. The data obtained support the idea that insulin monomers are the active species responsible for insulin action.

Drug Interactions↗