Material characterization of porcine lenticular soluble proteins.
The soluble proteins present in the ocular lens impart important optical and dynamic mechanical properties on the lens. The short-range order of crystallin proteins grants transparency to a very concentrated protein solution. This unique protein system directly enables proper visual function of the eye. These proteins were investigated in steady and oscillatory shear. Steady shear data were fitted with a modified Herschel-Bulkley yield stress model that allows for a Newtonian plateau at low shear rates. The Cox-Merz rule was used in conjunction with large amplitude oscillatory shear to give insight into the degradation of the fluid structure with increasing strain. The shear thinning viscoelastic behavior of these proteins gives rise to beneficial mechanical properties and results from the same short-range order granting optical transparency.
Reilly
Matthew A
MA
Department of Veterans Affairs, 915 North Grand Boulevard, St. Louis, Missouri 63106, USA.
Rapp
Brian
B
Hamilton
Paul D
PD
Shen
Amy Q
AQ
Ravi
Nathan
N
D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004548:Elasticity; D007525:Isoelectric Focusing; D007908:Lens, Crystalline / Q000737:chemistry*; D008954:Models, Biological; D009991:Oscillometry; D012212:Rheology; D033081:Shear Strength; D013314:Stress, Mechanical; D034421:Sus scrofa; D014783:Viscosity; D038201:alpha-Crystallins / Q000737:chemistry*; D038204:beta-Crystallins / Q000737:chemistry*; D038222:gamma-Crystallins / Q000737:chemistry*
D038201:alpha-Crystallins; D038204:beta-Crystallins; D038222:gamma-Crystallins