Isolation of Carbonic Anhydrase from Dog Erythrocytes and Determination of Its N-Terminal Amino-Acid Sequence
| Autor: | Ivan Kluh, Mohamed H. Soliman |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Erythrocytes
Phenylalanine Carboxypeptidases Benzoates Biochemistry Dogs Species Specificity Carbonic anhydrase Serine Animals Chymotrypsin Humans Histidine Amino Acid Sequence Disulfides Horses Amino Acids Peptide sequence Carbonic Anhydrases chemistry.chemical_classification Chromatography biology Tryptophan Electrophoresis Disc Nitro Compounds Amino acid Enzyme Activation Enzyme chemistry biology.protein Carboxypeptidase A Cattle Electrophoresis Polyacrylamide Gel Ultracentrifugation |
| Zdroj: | European Journal of Biochemistry. 44:611-615 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1974.tb03518.x |
| Popis: | 1 The major form of carbonic anhydrase from dog erythrocytes has been isolated and characterized by activity determination, disc-gel electrophoresis, ultracentrifugal and amino acid analysis. Phenylalanine was determined as the C-terminal amino acid of the enzyme. One –SH group per mole of the enzyme is accessible to the Ellman reagent [5,5′-dithiobis(2-nitrobenzoic acid)]. 2 The N-terminal hexapeptide of the dog carbonic anhydrase has been released by chymotryptic cleavage and the sequence Ac-Ser-Ser-Ser-Ser-Asn-Trp was determined by carboxypeptidase A digestion. |
| Databáze: | OpenAIRE |
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