Metal Binding and Catalytic Activity in Bovine Carbonic Anhydrase

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Metal binding and catalytic activity in bovine carbonic anhydrase.

Carbonic anhydrase was the earliest known zinc metallo-enzyme (4). It has been isolated from various sources, mainly mammalian red blood cells (see (5)). Although several methods for the preparation of highly active enzyme were described earlier, adequate purification was not achieved nor was the stoichiometry of zinc established (5). Recently, bovine erythrocyte carbonic anhydrase, homogeneous...

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Effects of pH and inhibitors on some properties related to metal binding in bovine carbonic anhydrase.

Carbonic anhydrase contains one firmly bound zinc ion per enzyme molecule (1). The metal ion, which can be dissociated in the presence of a chelating agent, is essential for catalytic activity, and it has been suggested that it is a part of the active site (2). Some other divalent metal ions also activate the metal-free enzyme. For example, Co2+ gives 45oj, of the activity of the native enzyme ...

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Thermodynamics of metal ion binding. 2. Metal ion binding by carbonic anhydrase variants.

The ability to construct molecular motifs with predictable properties in aqueous solution requires an extensive knowledge of the relationships between structure and energetics. The design of metal binding motifs is currently an area of intense interest in the bioorganic community. To date synthetic motifs designed to bind metal ions lack the remarkable affinities observed in biological systems....

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Blood carbonic anhydrase activity in the newborn.

Logan, R. W., Crooks, S. M., Hutchison, J. H., and Kerr, M. M. (1973). Archives of Disease in Childhood, 48, 256. Blood carbonic anhydrase activity in the newborn. Erythrocyte carbonic anhydrase activity was measured in 7 adults, 12 mature newborn infants, 12 preterm low birthweight infants, 9 'dysmature' infants, 33 infants with the respiratory distress syndrome (RDS), and 5 infants who had re...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1962

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)60295-9