Some observations on the zinc in carbonic anhydrase
- 1 January 1952
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 50 (3) , 429-432
- https://doi.org/10.1042/bj0500429
Abstract
Carbonic anhydrase kept as long as 32 days at 0[degree] and pH 7.4 in a solution of Zn65-containing Zn salts (plus glycine to prevent precipitation of the Zn) took up no significant amount of Zn65. When red blood cells were labelled in vitro with Zn65, little or none of the Zn which entered the red cell was firmly attached to the carbonic anhydrase. The inability of carbonic anhydrase to exchange its Zn with Zn ions and simple Zn compounds supported the view of Keilin and Mann that the metal which was an integral part of the enzyme molecule was firmly bound to the protein.Keywords
This publication has 6 references indexed in Scilit:
- The fate of some intravenously injected zinc compounds. 1. The determination of 65Zn in tissues. 2. The fate of injected zinc carbonate and phosphate and a zinc dithizone complexBiochemical Journal, 1950
- ZINC IN THE MAMMALIAN ORGANISM, WITH PARTICULAR REFERENCE TO CARBONIC ANHYDRASEPhysiological Reviews, 1949
- Carotenoids, vitamin A and 7-dehydrosteroid in the frog (Rana temporaria)Biochemical Journal, 1949
- Zinc in Human TissuesAmerican Journal of Clinical Pathology, 1947
- Some Experiments on chlorophyll and photosynthesis using radioactive tracersThe Journal of Physical Chemistry, 1942
- Carbonic anhydrase. Purification and nature of the enzymeBiochemical Journal, 1940