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. The precision of the method reveals the effects of fibril-attached matrix, when conventional methods of mechanical testing fail.
Kronick
P L
PL
U.S. Department of Agriculture, ARS, Eastern Regional Research Center, Philadelphia, PA 19118.
Sacks
M S
MS
D000818:Animals; D001696:Biomechanical Phenomena; D002417:Cattle; D002808:Chondroitin Lyases; D004548:Elasticity; D004594:Electrophysiology; D019855:Ethylene Glycol; D005026:Ethylene Glycols; D005069:Evaluation Studies as Topic; D005109:Extracellular Matrix / Q000737:chemistry / Q000502:physiology*; D006821:Hyaluronoglucosaminidase; D046911:Macromolecular Substances; D012867:Skin / Q000033:anatomy & histology* / Q000737:chemistry; D012879:Skin Physiological Phenomena; D013696:Temperature; D013997:Time Factors; D014357:Trypsin; D014783:Viscosity
D005026:Ethylene Glycols; D046911:Macromolecular Substances; D006821:Hyaluronoglucosaminidase; D014357:Trypsin; D002808:Chondroitin Lyases; D019855:Ethylene Glycol