| Literature DB >> 12739894 |
Sandra E Vairo Cavalli1, María C Arribére, Adriana Cortadi, Néstor O Caffini, Nora S Priolo.
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.Mesh:
Substances:
Year: 2003 PMID: 12739894 DOI: 10.1023/a:1023059525861
Source DB: PubMed Journal: J Protein Chem ISSN: 0277-8033