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Morrenain b I, a Papain-Like Endopeptidase from the Latex of Morrenia brachystephana Griseb. (Asclepiadaceae)

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Abstract

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.

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Authors and Affiliations

  1. LIPROVE, Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, C.C. 711, B1900AVW, La Plata, Argentina

    Sandra E. Vairo Cavalli, María C. Arribére, Néstor O. Caffini & Nora S. Priolo

  2. C´tedra de Botánica, Area Biología Vegetal, Departamento de Ciencias Biológicas, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 531, S2002LRK, Rosario, Argentina

    Adriana Cortadi

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  1. Sandra E. Vairo Cavalli
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  2. María C. Arribére
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  3. Adriana Cortadi
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  4. Néstor O. Caffini
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  5. Nora S. Priolo
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Correspondence to Sandra E. Vairo Cavalli.

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Vairo Cavalli, S.E., Arribére, M.C., Cortadi, A. et al. Morrenain b I, a Papain-Like Endopeptidase from the Latex of Morrenia brachystephana Griseb. (Asclepiadaceae). J Protein Chem 22, 15–22 (2003). https://doi.org/10.1023/A:1023059525861

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