Morrenain b I, a Papain-like Endopeptidase from the Latex of Morrenia brachystephana Griseb. (Asclepiadaceae)
| Autor: | Nora Priolo, Adriana Cortadi, Néstor O. Caffini, María Cecilia Arribére, Sandra Elizabeth Vairo Cavalli |
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| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Latex
Stereochemistry Cysteine Endopeptidases Biología Molecular Sequence Data plant endopeptidase Cysteine Proteinase Inhibitors Biochemistry Substrate Specificity Morrenia brachystephana cysteine proteinase chemistry.chemical_compound Enzyme Stability Papain Bioorganic chemistry Amino Acid Sequence chemistry.chemical_classification Hydrolysis Temperature Química Hydrogen-Ion Concentration PH profile Endopeptidase Apocynaceae Enzyme Activation Molecular Weight Enzyme chemistry Electrophoresis Polyacrylamide Gel Specific activity morrenain b I |
| Zdroj: | SEDICI (UNLP) Universidad Nacional de La Plata instacron:UNLP |
| Popis: | A new cysteine endopeptidase (morrenain b I) has been purified and characterized from the latex of stems and petiols of Morrenia brachystephana Griseb. (Asclepiadaceae). Morrenain b I was the minor proteolytic component in the latex but showed higher specific activity than morrenain b II, which was the main active fraction. Both enzymes showed similar pH profiles and molecular masses, but kinetic parameters and N-terminal sequences were quite distinct, demonstrating that they are different enzymes instead of different forms of the same enzyme. Centro de Investigación de Proteínas Vegetales |
| Databáze: | OpenAIRE |
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