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- W2050196716 abstract "1. 1. Carbonic anhydrase has been purified from erythrocytes of the European moose. Two forms (relative abundance, 4:1) with high specific activities (C-type) were separated by DEAE-cellulose chromatography. The moose appears to lack a low-activity (B-type) carbonic anhydrase in the blood which is similar to other ruminants. 2. 2. The purified major and minor forms appeared homogenous judging from polyacrylamide gel electrophoresis, ultracentrifugation and gel filtration experiments. The two forms have practically identical amino acid compositions. Each of them is composed of about 260 amino acid residues and one Zn 2− corresponding to a molecular weight of approx. 30 000. 3. 3. The physical and chemical properties of the major form of moose carbonic anhydrase are very similar to the corresponding properties of the bovine or sheep enzymes. The amino acid sequence of a section of the peptide chain, presumably comprising two of the metal-liganding histidyl residues, is -Leu-Val-Glx-Phe-His-Phe-His-Trp-Gly-, which is identical to the corresponding sequence in the bovine and sheep enzymes, The C-terminal sequence, -Leu-Arg. exhibits an inhomology in the penultimate position compared to other ruminant carbonic anhydrases, which could be explained by a single point mutation." @default.
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- W2050196716 date "1973-12-01" @default.
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- W2050196716 title "Purification and some properties of erythrocyte carbonic anhydrase from the European moose" @default.
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- W2050196716 doi "https://doi.org/10.1016/0005-2744(73)90435-x" @default.
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