Selective modification of tyrosine and cysteine residues in aspartate aminotransferase from pig heart cytosol
| Autor: | M.Ya. Karpeisky, T.V. Demidkina, O.L. Polyanovsky, Bocharov Al |
|---|---|
| Rok vydání: | 1973 |
| Předmět: |
Alkylation
Chemical Phenomena Transamination Stereochemistry Swine Biophysics In Vitro Techniques Biochemistry Maleimides chemistry.chemical_compound Cytosol Animals Trypsin Aspartate Aminotransferases Cysteine Sulfhydryl Compounds Tyrosine Molecular Biology Pyridoxal Amination chemistry.chemical_classification biology Myocardium Active site Sodium Dodecyl Sulfate Cell Biology Nitro Compounds Chemistry Enzyme chemistry biology.protein Spectrophotometry Ultraviolet Pyridoxamine |
| Zdroj: | Biochemical and biophysical research communications. 50(2) |
| ISSN: | 0006-291X |
| Popis: | In the region of the active site of aspartate amino-transferase two amino acid residues — one Tyr and one Cys — are accessible to selective modification by appropriate reagents. Modification of each of the two residues singly results in certain changes of the enzyme's physico-chemical properties, but does not abolish its ability to catalyse the transamination reaction. Complete inactivation, associated with irreversible amination of the protein-bound pyridoxal- P to pyridoxamine- P , is observed only on modification of both residues. |
| Databáze: | OpenAIRE |
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