Morrenain b I, a Papain-like Endopeptidase from the Latex of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>)
A new cysteine endopeptidase (morrenain b I) has been purified and characterized from the latex of stems and petiols of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>). Morrenain b I was the minor proteolytic component in the latex but showed higher specific ac...
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| Autores principales: | , , , , |
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| Formato: | Articulo |
| Lenguaje: | Inglés |
| Publicado: |
2003
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| Materias: | |
| Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/139496 |
| Aporte de: |
| Sumario: | A new cysteine endopeptidase (morrenain b I) has been purified and characterized from the latex of stems and petiols of <i>Morrenia brachystephana</i> Griseb. (<i>Asclepiadaceae</i>). 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. |
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