No abstract

Descemet's membrane, previously thought to be "structureless," has been found to be characterized by a fine structure of great regularity. Sections perpendicular to the plane of the membrane surface appeared to be cross-striated, with narrow dark bands separated by wide light bands traversed by fine filaments. Tangential sections showed a two-dimensional array of dark nodes and thin internodal filaments which connected each node with the six others around it to form a hexagonal figure. The average distance between nodes, and between the dark bands in transverse sections, was about 1070 A; the width of the nodes was about 270 A; and the width of the connecting filaments was less than 100 A. This pattern has been found in all species of Descemet's membrane so far examined, although it appeared to be better developed in some forms than in others. So far as is known, it has not been observed in any other type of tissue. The differentiation of Descemet's membrane has been followed in the chick embryo. It appeared late and developed slowly but showed the characteristic fine structure from the time it could be clearly identified. The evidence for placing Descemet's membrane in the collagen class of proteins is strongly supplemented by the results obtained from x-ray diffraction examination by Rougvie and Bear.

No abstract

Fibrils from certain molluscan muscles, in particular the adductor muscles of the clam Venus mercenaria, were examined with the electron microscope and found to possess periodic variations in structure. In order to make these structural variations visible, it was necessary to treat the fibrils with reagents of high electron scattering power (electron stains). Phosphotungstic acid was found to be particularly suitable. This stain combines with specific regions in the fibrils, forming a remarkably regular geometrical pattern of which the most prominent feature is a regular cross striation, representing a fiber-axis spacing of about 145A. Within each stained band, the stain is more highly concentrated in spots spaced about 193A from center to center across the band. A line drawn through any such spot parallel to the fiber axis passes through other similar spots, spaced five cross bands apart, making the length of the fiber-axis period precisely five times the fiber-axis spacing. X-ray diffraction data obtained by Bear from the intact muscles are compared with the electron microscope observations. The small angle diffractions are in close agreement with those which would be expected from the observed structure except for the magnitude of the lateral spacing. Electron microscope values for this spacing are significantly smaller than the 325A indicated by the x-ray data, probably as a result of lateral shrinkage in the vacuum-dried electron microscope specimens. No significant difference in axis spacing has been observed in fibrils isolated from muscles fixed with alcohol in contracted and extended states.