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Equilibrium species in cobalt(II) carbonic anhydrase

✍ Scribed by Bertini, Ivano; Lanini, G.; Luchinat, C.

Book ID
127120811
Publisher
American Chemical Society
Year
1983
Tongue
English
Weight
365 KB
Volume
105
Category
Article
ISSN
0002-7863

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The results of a study on the interaction between cobalt(II) bovine carbonic anhydrase and the a-amino acids L(s) and D(-Manine. glycine and betaine are reported\_ L(+)ahnine and glycine base been found to have larger aftinity for the enzyme than II(-) alanine whereas no sizable affinity is shown by

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The affinity of bicarboxylate ions (from oxaiate to glutarate) for cobalt(E) bovine carbonic anhydrase has been investigated and compared with that cf acetate and propionate. The oxalate ion shows a much greater affiiity for the enzyme than acetate. whereas the other bicarboxylate ions have very lit