High active isoenzyme of carbonic anhydrase in rat calvaria osteoclasts
✍ Scribed by H. K. Väänänen; E. -K. Parvinen
- Book ID
- 104786948
- Publisher
- Springer
- Year
- 1983
- Tongue
- English
- Weight
- 756 KB
- Volume
- 78
- Category
- Article
- ISSN
- 1432-119X
No coin nor oath required. For personal study only.
✦ Synopsis
Calvaria from newborn rats were used to localize carbonic anhydrase isoenzymes in bone tissue. Highly sensitive peroxidase-antiperoxidase method revealed strong reaction of high-active C form of carbonic anhydrase exclusively in the osteoclasts. There was no reaction in osteoblasts or fibroblasts but some population of bone marrow cells was positive. Isoenzyme B was found only in bone marrow cells. On the basis of the present and previous studies it is highly probable that carbonic anhydrase may have some crucial role in osteoclast mediated bone resorption. Carbonic anhydrase C may also be a suitable probe for studies of osteoclast function and origin.
📜 SIMILAR VOLUMES
Human and rat spermatozoa were stained for different carbonic anhydrase (CA) isoenzymes using specific antisera to human CA I, II and VI in conjunction with the immunofluorescence technique. The spermatozoa of both species were found to contain only CA II, which was located principally in the postac
Eighteen mate Sprague Dawley rats were divided into three groups. They were offered a semisynthetic casein diet containin, 0 either 1.2 mg &/kg dry matter (depletion group) or 100 mg &t/kg dry matter (ad Zibitum and pair-fed control groups). At the beginning and on the 5th and 24th day of the experi
The placenta has multiple functions, being the organ which provides oxygen and nutrients to the developing conceptus. In the placenta, the enzyme carbonic anhydrase (CA) may provide ions for exchange with Na+, K+, and Cl- in transepithelial movement of ions and fluid, as well as facilitating carbon