Calcification of alpha-elastin coacervates: a bulk property of elastin.
Scanning electron microscopy and electron probe microanalysis studies are reported on thin sections of calcified coacervates of alpha-elastin. It is found that the capacity of elastin coacervates to initiate calcification is a bulk property of the coacervate and not limited to the serum-coacervate interface, that the calcium phosphate deposits act to bind the protein units together and slow the dissolution and spreading of the coacervate as it floats on an airwater interface, and that, within the limits of detectability, there is no involvement of sulfur. As the charged groups of alpha-elastin had been blocked, the initiation of deposition is due to neutral sites in the protein which are tightly bound to the calcium phosphate deposits.
D000818:Animals; D001665:Binding Sites; D002113:Calcification, Physiologic; D002130:Calcium Phosphates; D003102:Colloids; D004549:Elastin; D004577:Electron Probe Microanalysis; D008855:Microscopy, Electron, Scanning; D013552:Swine
D002130:Calcium Phosphates; D003102:Colloids; D004549:Elastin