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- W2116531544 abstract "In 1928, studies on the rate of escape of carbon dioxide from hemolyzed blood led to the recognition of a red cell substance catalyzing the reversible hydration of CO2 [12]. By 1932, the substance was shown to be an enzyme and given the name carbonic anhydrase [26, 27]. In the following 10 years the enzyme was partially purified [28], shown to be a zinc-containing enzyme [15, 16] having a molecular weight of about 30,000 [33] and to contain one zinc ion per enzyme molecule [37]. World War II and its aftermath interrupted research on carbonic anhydrase for almost 20 years, but in the early 60’s researchers in Sweden [23, 30] reported several homogenous preparations of the enzyme which differed in electrophoretic mobility and specific activity. These observations were quickly confirmed by others [18, 34, 35] with the resulting realization that human erythrocytes contained several different enzyme forms catalyzing the reversible hydration of carbon dioxide." @default.
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- W2116531544 date "1980-01-01" @default.
- W2116531544 modified "2023-09-27" @default.
- W2116531544 title "Primary Structure of Carbonic Anhydrases" @default.
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- W2116531544 doi "https://doi.org/10.1007/978-3-642-67572-0_17" @default.
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