The self-association of zinc-free bovine insulin. A single model based on interactions in the crystal that describes the association pattern in solution at pH 2, 7 and 10

Mark, AE, Nichol, LW and Jeffrey, PD (1987) The self-association of zinc-free bovine insulin. A single model based on interactions in the crystal that describes the association pattern in solution at pH 2, 7 and 10. Biophysical Chemistry, 27 2: 103-117. doi:10.1016/0301-4622(87)80051-0


Author Mark, AE
Nichol, LW
Jeffrey, PD
Title The self-association of zinc-free bovine insulin. A single model based on interactions in the crystal that describes the association pattern in solution at pH 2, 7 and 10
Journal name Biophysical Chemistry   Check publisher's open access policy
ISSN 0301-4622
Publication date 1987-01-01
Year available 1987
Sub-type Article (original research)
DOI 10.1016/0301-4622(87)80051-0
Open Access Status Not yet assessed
Volume 27
Issue 2
Start page 103
End page 117
Total pages 15
Place of publication AMSTERDAM
Publisher ELSEVIER SCIENCE BV
Language eng
Subject 1303 Specialist Studies in Education
1304 Biophysics
1606 Political Science
Abstract Sedimentation equilibrium studies are used to establish that a new pattern for the self-association of zinc-free insulin in solution is applicable over a wide range of conditions of pH, ionic strength and temperature. In this pattern, which is based on information from the existing literature on the X-ray crystal structure of insulin, the insulin monomer is viewed as having two distinct faces both capable of self- interaction. Sedimentation equilibrium experiments were analysed using expressions formulated for this association pattern that describe the dependence of weight average molecular weight and monomer concentration on total protein concentration. It has thereby been possible to obtain values for the two association constants which govern the system for each set of conditions studied, due allowance having been made for composition dependent non-ideality effects. Furthermore, by relating the pH, temperature and ionic strength dependence of the association constants with properties of various amino acid residues on the surface of the insulin monomer, it has also been possible to assign tentatively each constant to a particular reaction domain.
Keyword Indefinite self-association
Insulin
Insulin association pattern
Sedimentation equilibrium
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: ResearcherID Downloads - Archived
 
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