Summary
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.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Anzenbacher P., Kalous V.: Binding of D-glucose to insulin — Biochim. biophys. Acta (Amst.)386, 603, 1975.
Anzenbacher P., Kalous V.: Komůrkový aparát pro rovnovážnou dialysu — Chem. Listy69, 880, 1975.
Blundell T. L., Dodson G. G., Dodson E. J., Hodgkin D. C., Vijayan M.: Insulin, its chemistry and biochemistry — Recent Progr. Hormone Res.27, 1, 1971.
Cuatrecasas P.: Insulin receptors of liver and fat cell membranes — Fed. Proc.32, 1838, 1973.
Czech M. P.: Molecular basis of insulin action — Ann. Rev. Biochem.46, 359, 1977.
Dahlquist F. W.: The quantitative interpretation of maximum in Scatchard plot — FEBS Letters49, 267, 1974.
Grant P. T.: The conversion of proinsulin into insulin in the β-cells of mammals and fishes — Biochem. J.125, 49P, 1971.
Henis Y. I., Levitzki A.: An analysis on the slope of Scatchard plots — Europ. J. Biochem.71, 529, 1976.
Hollenberg M. D., Cuatrecasas P.: Insulin interaction with membrane receptors and relationship to cyclic purine nucleotides and cell growth — Fed. Proc.34, 1556, 1975.
Jeffrey P. D.: Polymerization behavior of bovine zinc-insulin at neutral pH. Molecular weight of the subunit and the effect of glucose — Biochemistry (Wash.)13, 4441, 1974.
Kahn C. R., Neville D. M. Jr., Roth J.: Insulin-receptor interaction in the obese hyperglycemic mouse. A model of insulin resistance — J. biol. Chem.248, 244, 1973.
Klotz I. M.: Protein interactions with small molecules — Acc. Chem. Res.7, 162, 1974.
Levitzki A., Schlessinger J.: Cooperativity in associating proteins. Monomer-dimer equilibrium coupled to ligand binding — Biochemistry (Wash.)13, 5214, 1974.
Maturo J. M. III: Isolation and partial characterization of a tryptophan-insulin complex — Endocrinology90, 947, 1972.
Maturo J. M. III, Diloff S.: Interaction between amino acids and insulin — Hormone metab. Res.5, 54, 1973.
Milthorpe B. K., Nichol L. W., Jeffrey P. D.: The polymerization pattern of zinc(2)-insulin at pH 7.0 — Biochim. biophys. Acta (Amst.)495, 195, 1977.
Nichol L. W., Jackson W. J. H., Winzor D. J.: A theoretical study of the binding of small molecules to a polymerizing protein system. A model for allosteric effects — Biochemistry (Wash.)6, 2449, 1967.
Pullen R. A., Lindsay D. C., Wood S. P., Tickle I. S., Blundell T. L., Wollmer A., Krail G., Brandenburg D., Zahn H., Gliemann J., Gammeltoft S.: Receptor-binding region of insulin — Nature (Lond.)259, 369, 1976.
Scatchard G.: The attractions of proteins for small molecules and ions — Ann. N.Y. Acad. Sci.51, 660, 1949.
Scholtan W.: Die Bindung der Sulfonamide an Eiweisskörper — Arzneimittel-Forsch.14, 1139, 1964.
Schwarz G.: Some general aspects regarding the interpretation of binding data by means of a Scatchard plot — Biophys. Struct. Mechanism2, 1, 1976.
Steinhardt J., Reynolds J. A.: Multiple equilibria in proteins — Academic Press, New York, 1969; p. 10.
Yalow R. S., Berson S. A.: Big, big insulin — Metabolism22, 703, 1973.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kalous, V., Anzenbacher, P. On the mechanism of the insulin-glucose interactions. Acta diabet. lat 16, 169–174 (1979). https://doi.org/10.1007/BF02581096
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF02581096