Some observations on the fine structure of elastoidin.
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Animals↗
Biomedical subjects
D P Knight
Publications and source records attributed to D P Knight.
Amianthoid change: orientation of normal collagen fibrils during aging.
High-angle x-ray diffraction provides direct evidence that amianthoid change, occurring during aging of costal cartilage, corresponds to a transformation from an isotropic to a marked anisotropic distribution of collagen fibrils. Low-angle x-ray diffraction and electron microscopy show that the fibrils have the customary 67-nanometer axial periodicity. Electron microscopy shows that wide amianthoid collagen fibrils consist of smaller parallel fibrils fused together. Similarities between amianthoid change and tendon morphogenesis are briefly discussed. Amianthoid change is remarkable in that aging is accompanied by increased order.
Aging↗
Fine structure of the dogfish egg case: a unique collagenous material.
The fine structure of the dogfish egg case is described with special reference to the highly ordered, unique, collagen-containing fibrils. The outer layer of the case wall contains densely packed, amorphous granules, rich in tyrosine while approximately 98% of the thickness of the case is built up from orthogonally stacked laminae of closely packed, collagen-containing fibrils. These fibrils show a paracrystalline three-dimensional construction. A model for the structure of the B band of the fibril is proposed, based on appearances in transverse sections of different thickness and on two projection seen in longitudinal sections. The transverse projection of the unit cell appears to be a square lattice with sides approximately 110 A possibly containing a pseudocell with sides (see article). The structure of these fibrils is discussed in relation to those of rat tail tendon collagen.
Animals↗
Negative staining of rat tail tendon collagen fibrils with uranyl formate.
Negative staining of rat tail tendon collagen fibrils with uranyl formate appears to reveal more detail in the axial banding pattern than any other positive or negative staining method hitherto employed. In addition, uranyl formate and other uranyl solutions appear to reveal fine, closely spaced, longitudinal filaments which may represent the individual tropocollagen molecules.
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