Skip to main content

. 1946;40(2):319–330. doi: 10.1042/bj0400319

The effect of substrate concentration, pH and other factors upon the activity of carbonic anhydrase

F J W Roughton ¹, V H Booth ¹

PMCID: PMC1258342 PMID: 16748007

330

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

Booth V. H. Carbonic anhydrase activity inside corpuscles. Enzyme-substrate accessibility factors. J Physiol. 1938 Jul 14;93(2):117–128. doi: 10.1113/jphysiol.1938.sp003630. [DOI] [PMC free article] [PubMed] [Google Scholar]
Brinkman R. The occurrence of carbonic anhydrase in lower marine animals. J Physiol. 1933 Dec 5;80(2):171–173. doi: 10.1113/jphysiol.1933.sp003079. [DOI] [PMC free article] [PubMed] [Google Scholar]
Dirken M. N., Mook H. W. The rate of gas exchange between blood cells and serum. J Physiol. 1931 Dec 17;73(4):349–360. doi: 10.1113/jphysiol.1931.sp002816. [DOI] [PMC free article] [PubMed] [Google Scholar]
Keilin D., Mann T. Carbonic anhydrase. Purification and nature of the enzyme. Biochem J. 1940 Sep;34(8-9):1163–1176. doi: 10.1042/bj0341163. [DOI] [PMC free article] [PubMed] [Google Scholar]
Mann P. J., Woolf B. The action of salts on fumarase. I. Biochem J. 1930;24(2):427–434. doi: 10.1042/bj0240427. [DOI] [PMC free article] [PubMed] [Google Scholar]
Meldrum N. U., Roughton F. J. Carbonic anhydrase. Its preparation and properties. J Physiol. 1933 Dec 5;80(2):113–142. doi: 10.1113/jphysiol.1933.sp003077. [DOI] [PMC free article] [PubMed] [Google Scholar]
Roughton F. J., Booth V. H. The manometric determination of the activity of carbonic anhydrase under varied conditions. Biochem J. 1946;40(2):309–319. doi: 10.1042/bj0400309. [DOI] [PMC free article] [PubMed] [Google Scholar]

ACTIONS

RESOURCES