Primary structure of mitochondrial glutamic oxaloacetic transaminase from rat liver : comparison with that of the pig heart isozyme
| Autor: | Hiroshi Wada, Ryuzo Sakakibara, Quang Khai Huynh, Takehiko Watanabe |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Swine
Biophysics Homoserine Mitochondria Liver Biology Cleavage (embryo) Biochemistry Isozyme chemistry.chemical_compound Species Specificity Animals Amino Acid Sequence Aspartate Aminotransferases Cyanogen Bromide Molecular Biology Peptide sequence Methionine Myocardium Protein primary structure Cell Biology Molecular biology Peptide Fragments Rats Isoenzymes Cytosol chemistry Organ Specificity Cyanogen bromide |
| Zdroj: | Biochemical and biophysical research communications. 97(2) |
| ISSN: | 0006-291X |
| Popis: | The complete amino acid sequence of the mitochondrial glutamic oxaloacetic transaminase isozyme from rat liver is presented. The sequence contained 401 amino acid residues, 10 of which are methionine. Cyanogen bromide cleavage of mitochondrial glutamic oxaloacetic transaminase produced 12 peptides, one of which contained an internal homoserine residue resulting from incomplete cleavage by cyanogen bromide. The calculated molecular weight was 44,358. The sequence showed 94% homology with that of the corresponding isozyme from pig heart. These findings support the conclusion that the rate of evolution of the mitochondrial isozymes is lower than that of their cytosolic isozymes. |
| Databáze: | OpenAIRE |
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