These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Evidence of a high-activity C type of carbonic anhydrase in human ciliary processes.
    Author: Wistrand PJ, Garg LC.
    Journal: Invest Ophthalmol Vis Sci; 1979 Aug; 18(8):802-6. PubMed ID: 110722.
    Abstract:
    Carbonic anhydrase activity was found in the ciliary process of fresh human donor eyes, originating from an enzyme antigenically similar to the erythrocyte high-activity isoenzyme HCA C. It was sensitive to inhibition by acetazolamide and resistant to inhibition by halides like HCA C. The enzyme is probably identical with HCA C. Its tissue concentration was one fifth to one tenth of that in the human kidney. The erythrocyte low-activity isoenzyme HCA B was also found in the processes as a contaminant.
    [Abstract] [Full Text] [Related] [New Search]