Scanning Electron Microscope Observatlons on Elastin

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Abstract
Samples of bovine Ligamenturn Nuchae elastin have been examined by scanning electron niicroscopy, both in the native state and after purification from contaminating components. The elastic substance appears coniposed of fibers, about 6 μ in diameter, embedded in an amorphous matrix which is removed by purification. They arc chiefly oriented along the main axis of the Ligamenturn, and often interwoven, branched and twisted. In many cases, smaller fibrillar components, either 1 μ or 0.2 μ in average diameter, have been observed. The analysis has been extended to samples of purified elastin swollen in water, methanol, triRuoroethanol and diniethylsulphoxide, longitudinally or two-dimensionally stretched and then dried under tension. It has been found that each single fiber may be stretched up to 300% of its original length before failure, a value much higher than the maximum elongation observed for macroscopic samples (80 %). The results, which indicate that elastin is not a homogeneous system at different levels of organization, have been discussed on the basis of our previous analyses of the X-ray and other physical properties of elastin.