Rate constant for insulin dimerization

Value 1e+8 M^-1×sec^-1
Organism Pig Sus species
Reference Northrup SH, Erickson HP. Kinetics of protein-protein association explained by Brownian dynamics computer simulation. Proc Natl Acad Sci U S A. 1992 Apr 15 89(8):3338-42. p.3338 left column bottom paragraphPubMed ID1565624
Primary Source [6] Koren, R. & Hammes, G. G. (1976) A kinetic study of protein-protein interactions. Biochemistry 15, 1165- 1170.PubMed ID3211
Method Primary source [6] abstract: "Kinetic studies have been carried out of the monomer-dimer interaction of insulin, beta-lactoglobulin, and alpha-chymotrypsin using stopped-flow and temperature-jump techniques. The pH indicators bromothymol blue, bromophenol blue, and phenol red were used to monitor pH changes associated with the monomer-dimer interaction." Primary source studied porcine insulin
Comments p.3338 left column bottom paragraph: "Faster bimolecular rates have been reported (primary source) for insulin dimerization (k2 = 10^8 M^-1×s^-1) and for interaction of cytochrome c with cytochrome c peroxidase (ref 7) and cytochrome b5 (ref 8) (k2 varies from 10^7 to 10^9, with the faster rates at low ionic strength). These very fast reactions are the results of strong attractive coulombic forces that highly favor formation of the productive reaction complexes (refs 8-11)."
Entered by Uri M
ID 112540