December 1974
Volume 13, Issue 12
Free
Articles  |   December 1974
An Insoluble Structural Glycoprotein a Major Constituent of the Zonula Zinni
Author Affiliations
  • ZACHARIAS DISCHE
    Department of Ophthalmology, College of Physicians and Surgeons, Columbia University, New York, N. Y., 10032
  • V. L. MURTY
    Department of Ophthalmology, College of Physicians and Surgeons, Columbia University, New York, N. Y., 10032
Investigative Ophthalmology & Visual Science December 1974, Vol.13, 991-995. doi:
  • Views
  • PDF
  • Share
  • Tools
    • Alerts
      ×
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      ZACHARIAS DISCHE, V. L. MURTY; An Insoluble Structural Glycoprotein a Major Constituent of the Zonula Zinni. Invest. Ophthalmol. Vis. Sci. 1974;13(12):991-995.

      Download citation file:


      © ARVO (1962-2015); The Authors (2016-present)

      ×
  • Supplements
This content is PDF only. Please click on the PDF icon to access.
Abstract

Experiments were carried out to determine the localization of the insoluble structural glycoprotein ivhich remains after exhaustive degradation of the bovine and rabbit lens capsules with high-purity collagenase. The material can be extracted from the residue with 0.1 M β-mercaptoethanol at room temperature. Most of this material was shown to be present in the capsule of the equatorial region of the lens. Furthermore, preparations of lens capsule containing the extracapsular* fibrils of zonula Zinni were shown to contain about as much of this structural glycoprotein as the whole capsule itself. The glycoprotein appears to be a major constituent of the zonula fibrils and the compositibn of its carbohydrate suggests a close relationship to the glycoprotein of the vitreous body previously obtained in our laboratory as an insoluble precipitate after degradation of the hyaluronic acid of the vitreous.

×
×

This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.

×