Purification and characterization of cathepsin d-like proteinase from the tadpole tail of bullfrog, Rana catesbeiana
| Autor: | Ken-ichiro Kobayashi, Masato Nanbu, Shiro Horiuchi |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Tail
Physiology Cathepsin D Biochemistry Substrate Specificity chemistry.chemical_compound Pepstatins Animals Sodium dodecyl sulfate Molecular Biology Polyacrylamide gel electrophoresis Gel electrophoresis chemistry.chemical_classification Rana catesbeiana Chromatography biology Substrate (chemistry) General Medicine Hydrogen-Ion Concentration Enzyme assay Molecular Weight Kinetics Enzyme chemistry Larva biology.protein Pepstatin |
| Zdroj: | Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 89:569-575 |
| ISSN: | 0305-0491 |
| DOI: | 10.1016/0305-0491(88)90176-9 |
| Popis: | 1. 1. An acid aspartic proteinase in the regressing tadpole tail was purified about 800-fold with a 36% recovery. 2. 2. The mol. wt of the enzyme was found to be 42,000 on gel filtration and 38,000 on sodium dodecyl sulfate polyacrylamide gel electrophoresis, respectively. 3. 3. The purified enzyme had a maximum activity at pH 3.5 and an apparent K m of 0.084% with acid-denatured hemoglobin as substrate. 4. 4. The enzyme activity was strongly inhibited by pepstatin. In addition, diazoacetylnorleucine methyl ester inactivated the enzyme in the presence of cupric ions. 5. 5. The enzyme was identified as a cathepsin D (EC. 3.4.23.5)-like proteinase. |
| Databáze: | OpenAIRE |
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