Gel Filtration using a Column packed with Elastin Fibres

Abstract

THE molecular architecture of elastin as it exists in the water-swollen fibre is ill understood, but to account for the insolubility, rubber-like elasticity and swelling properties of the wet protein fibre its structure is regarded as a crosslinked gel. Chemical studies have shown that the peptide chains are organized as a three-dimensional network, crosslinked at intervals by covalent bonds^1,2, and it has become usual to assume that between these links the chains are hydrated and in intimate contact with the swelling water. Studies of the rubber-like stress–strain characteristics of the wet fibres³ indicate that there is no crystallinity, and suggest that the chains between the crosslinks adopt a randomly crumpled conformation due to unrestricted thermal motion. In view of the large amounts of amino-acid with non-polar side-chains in elastin⁴ it seems possible that sites of hydrophobic interaction of considerable size may occur in the network. Such a “corpuscular” model of elastin structure has recently been proposed to account for the behaviour of elastin with enzymes and for the course of fibrogenesis^5,6. The distribution of the swelling water in the gel would be expected to have a marked influence on the behaviour of solute molecules diffusing in the water spaces, and the purpose of the present work was to examine the behaviour of such solutes using a chromatographic method.