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Partial amino acid sequence of erythrocyte carbonic anhydrase from tiger shark

May 31, 2017 | Autor: U. Carlsson | Categoría: Physiology, Humans, Sharks, HPLC, Animals, Trypsin, Comparative Biochemistry and Physiology, High Pressure Liquid Chromatography, Amino Acids, Carbonic anhydrase, Alkylation, Species Specificity, Amino Acid Sequence, Quntitative Thin Layer Chromatography, Liquid Scintillation Counting, Erythrocytes, Isozyme, Dogfish, Biochemistry and cell biology, Molecular Sequence Data, Trypsin, Comparative Biochemistry and Physiology, High Pressure Liquid Chromatography, Amino Acids, Carbonic anhydrase, Alkylation, Species Specificity, Amino Acid Sequence, Quntitative Thin Layer Chromatography, Liquid Scintillation Counting, Erythrocytes, Isozyme, Dogfish, Biochemistry and cell biology, Molecular Sequence Data
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Descripción

1. A partial primary structure (197 residues) of carbonic anhydrase from tiger shark (Galeocerdo cuvieri) erythrocytes has been determined. 2. The amino acid sequence of the enzyme is identical to those of human cytoplasmic carbonic anhydrases (CA I-III) by as much as 52-60%. 3. It is shown that tiger shark CA most closely resembles the CA II isoenzyme of amniotes. 4. Isoelectric focusing and inhibition studies on carbonic anhydrase from dogfish (Squalus acanthias) blood and muscle indicate the presence of the same isoenzyme in shark blood and muscle.
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