35Cl and 81Br Nuclear Magnetic Resonance Studies of Carbonic Anhydrase
Mammalian erythrocytes often contain more than one type of carbonic anhydrase and human erythrocytes in particular yield two prinicpal forms of the enzyme, which are distinguished foremost by their relative specific activities in regards to the catalysis of the important reversible carbon dioxide hydration reaction. Although these isozymes exhibit many other differences, they have in common the stringent requirement of one zinc ion per molecular weight unit of about 30,000.
KeywordsZinc Hydrolysis Dioxide Hydration Cobalt
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- 4.Notstrand B, Vaara I, Kannan KK (1975) Structural relationship of human erythrocyte carbonic anhydrase isozymes B and C. In: Markert CL (ed) Proc Int Conf Isozymes, vol I. Molecular structure. Academic Press, London New York, p 575Google Scholar
- 5.Riddiford LM (1965) Acid difference spectra of human carbonic anhydrases. J Biol Chem 240: 168–172Google Scholar
- 6.Roughton FJW, Booth VH (1946) Manometric determination of the activity of carbonic anhydrase under varied conditions. Biochem J 40: 309–319Google Scholar
- 14.Whitney PL, Brandt H (1976) Effects of two ionizing groups on the active site of human carbonic anhydrase B. J Biol Chem 251: 3862–3867Google Scholar