April 1992
Volume 33, Issue 5
Free
Articles  |   April 1992
Characterization of cholinesterase activities in primary cultures of retinal pigment epithelium.
Author Affiliations
  • R Salceda
    Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, D.F.
  • G Sánchez
    Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, D.F.
  • J M León-Cázares
    Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, D.F.
Investigative Ophthalmology & Visual Science April 1992, Vol.33, 1690-1695. doi:
  • Views
  • PDF
  • Share
  • Tools
    • Alerts
      ×
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      R Salceda, G Sánchez, J M León-Cázares; Characterization of cholinesterase activities in primary cultures of retinal pigment epithelium.. Invest. Ophthalmol. Vis. Sci. 1992;33(5):1690-1695.

      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

This report presents a comparative description of the acetylcholinesterase and butyrylcholinesterase activities and their molecular forms in primary cultures of retinal pigment epithelium (RPE). Acetylcholinesterase activity increases during differentiation of the cells. Sucrose sedimentation analysis of acetylcholinesterase and butyrylcholinesterase molecular forms revealed the presence of A12, G4, G2, and G1 and A8, G4, G2 and G1, respectively. RPE cells in culture release both cholinesterases into the growth medium, sedimenting as the G4 molecular form. Changes in the molecular forms of both enzymes were observed during differentiation. The results suggest a possible relationship between butyrylcholinesterase activity and cell proliferation and acetylcholinesterase activity and cell differentiation.

×
×

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.

×