作者: Ismael Rodrigo , Pablo Vera , Leendert C. Van Loon , Vicente Conejero
DOI: 10.1104/PP.95.2.616
关键词: Extracellular 、 Enzyme 、 Pathogenesis-related protein 、 Biochemistry 、 Proteinase 3 、 Proteases 、 Biology 、 Nicotiana tabacum 、 Molecular mass 、 Protein turnover
摘要: Tobacco (Nicotiana tabacum L.) leaves were found to contain an extracellular proteinase that endoproteolytically cleaves tobacco pathogenesis-related (PR) proteins. This was partially purified from and characterized as aspartyl with a pH optimum around 3 molecular mass of 36,000 40,000 daltons. In vitro, the enzyme cleaved tomato PR proteins into discrete fragments. The characteristics this similar pepsin identical those displayed by previously described 37-kilodalton active against (I Rodrigo, P Vera, V Conejero [1989] Eur J Biochem 184: 663-669), suggesting these proteases could play role in conserved mechanism for protein turnover plants.