The Catalytic Versatility of Erythrocyte Carbonic Anhydrase. I. Kinetic Studies of the Enzyme-Catalyzed Hydration of Acetaldehyde*

Y. Pocker; J. E. Meany

doi:10.1021/bi00887a037

journal article Nov 01, 1965

The Catalytic Versatility of Erythrocyte Carbonic Anhydrase. I. Kinetic Studies of the Enzyme-Catalyzed Hydration of Acetaldehyde*

Y. Pocker J. E. Meany

Biochemistry Vol. 4 No. 11 pp. 2535-2541 · American Chemical Society (ACS)

View at Publisher Save 10.1021/bi00887a037

Topics

No keywords indexed for this article. Browse by subject →

Cited By

64

Structural properties of human carbonic anhydrase II at pH 9.5

Satish K. Nair, David W. Christianson · 1991

Biochemical and Biophysical Researc...

Localization of lysines acetylated in ubiquitin reacted with p-nitrophenyl acetate

Jack R. Jabusch, H.F. Deutsch · 1985

Archives of Biochemistry and Biophy...

Evaluation of the two‐substrate pathway of glyoxalase I from yeast by use of carbonic anhydrase and rapid‐kinetic studies

Ewa Marmstål, Bengt Mannervik · 1981

FEBS Letters

Crystal Structure of Human Carbonic Anhydrase C

A. Liljas, K. K. Kannan · 1972

Nature New Biology

Facilitated Proton Transfer in Enzyme Catalysis

Jui H. Wang · 1968

Science

Metrics

64

Citations

0

References

Details

Published: Nov 01, 1965
Vol/Issue: 4(11)
Pages: 2535-2541

Authors

Cite This Article

Y. Pocker, J. E. Meany (1965). The Catalytic Versatility of Erythrocyte Carbonic Anhydrase. I. Kinetic Studies of the Enzyme-Catalyzed Hydration of Acetaldehyde*. Biochemistry, 4(11), 2535-2541. https://doi.org/10.1021/bi00887a037

The Catalytic Versatility of Erythrocyte Carbonic Anhydrase. I. Kinetic Studies of the Enzyme-Catalyzed Hydration of Acetaldehyde*

You May Also Like