Thermal stabilization of collagen fibers by calcification.

Mineralized collagenous tissue is known to be more stable than soft collagenous tissue both mechanically and thermally. We find that the denaturation temperature of collagen in bone scanned in differential scanning calorimetry at 5 degrees C/min is 155 degrees C, 90 degrees C higher than that in skin. Furthermore, when the bone is partially demineralized with citrate, a discrete intermediate denaturation temperature appears at 113 degrees C, indicating that the mineral is retained at preferential binding sites in the collagen until it is completely leached out.

Matrix macromolecules that affect the viscoelasticity of calfskin.

The chemical basis of viscoelasticity of bovine skin was explored by mechanical relaxation spectroscopy after selective enzymatic degradation. Measurements covered a wide range of time scales because water was replaced in the tissue with aqueous mixtures of ethylene glycol, which maintained a water-like electrical environment for the charged macromolecules down to -50 degrees C. Macromolecular components that couple the fibrils to the interfibrillar matrix contribute about half the values of the resultant storage and loss moduli, while removal of components that are readily extractable, so perhaps free in the matrix, did not alter these mechanical quantities or their relaxations.

Quantification of vertical-fiber defect in cattle hide by small-angle light scattering.

Vertical-fiber defect (VFD), an abnormal arrangement of collagen fibers in hides of certain cattle breeds, is still not fully understood. Prior work has been limited to subjective histological examinations from hide biopsies. A device using small angle light scattering (SALS) was used to quantify the collagen fiber orientation of sections taken from hide biopsies.

Analysis of the effects of pH and tensile deformation on the small-deformation modulus of calf skin.

A dynamic technique was used to measure the elastic modulus of the reticular dermis of calf skin at a small (0.1%), non-perturbing oscillating deformation. The elastic modulus increases by over an order of magnitude when the tissue is stretched by only 10% before the measurement is made.

The locations of collagens with different thermal stabilities in fibrils of bovine reticular dermis.

The techniques of differential scanning calorimetry and electron microscopy were combined to locate collagens with different thermal stabilities in bovine dermis. When calfskin was heated at 1.25 degrees C/min, denatured cores developed in the fibrils at 65 degrees C, leaving native-banded sheaths.