Literature DB >> 18471013

Material characterization of porcine lenticular soluble proteins.

Matthew A Reilly1, Brian Rapp, Paul D Hamilton, Amy Q Shen, Nathan Ravi.   

Abstract

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.

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Year:  2008        PMID: 18471013     DOI: 10.1021/bm701229t

Source DB:  PubMed          Journal:  Biomacromolecules        ISSN: 1525-7797            Impact factor:   6.988


  3 in total

1.  In vitro interactions of histones and α-crystallin.

Authors:  Paul D Hamilton; Usha P Andley
Journal:  Biochem Biophys Rep       Date:  2018-06-01

2.  Creatine kinase/α-crystallin interaction functions in cataract development.

Authors:  Paul D Hamilton; Stephanie L Bozeman; Usha P Andley
Journal:  Biochem Biophys Rep       Date:  2020-02-29

3.  Lens Stretching Modulates Lens Epithelial Cell Proliferation via YAP Regulation.

Authors:  Bharat Kumar; Heather L Chandler; Timothy Plageman; Matthew A Reilly
Journal:  Invest Ophthalmol Vis Sci       Date:  2019-09-03       Impact factor: 4.799

  3 in total

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