Immunohistochemical demonstration of carbonic anhydrase isoenzyme C in the epithelium of the human ciliary processes
โ Scribed by T. Kumpulainen
- Publisher
- Springer
- Year
- 1983
- Tongue
- English
- Weight
- 749 KB
- Volume
- 77
- Category
- Article
- ISSN
- 1432-119X
No coin nor oath required. For personal study only.
โฆ Synopsis
Extravascular location of two main carbonic anhydrase isoenzymes was immunohistochemically investigated in human ciliary processes. The high-activity carbonic anhydrase isoenzyme C was clearly demonstrated in the ciliary epithelium, but was absent from the ciliary stroma. The low-activity isoenzyme B was evident neither in the epithelium nor in the stroma.
๐ SIMILAR VOLUMES
Alkaline hepatic bile is acidified in the gallbladder to prevent calcium precipitation and gallstone formation. Because membrane-bound carbonic anhydrase (CA) isoenzyme IV participates with cytoplasmic CA II in the acidification of urine in the kidney, we studied its expression in different regions
A monoclonal antibody (RBU/01) was raised against human thyroglobulin and its suitability for the immunohistochemical staining of thyroglobulin was determined on fixed, wax-embedded tissue, using the peroxidase anti-peroxidase (PAP) method. The antibody was then used to demonstrate the expression of