Biochemical and PMF MALDI-TOF Analyses of Two Novel Papain-Like Plant Proteinases

Title: Biochemical and PMF MALDI-TOF Analyses of Two Novel Papain-Like Plant Proteinases

Volume: 16 Issue: 11

Author(s): W. D. Obregon, C. S. Liggieri, S. R. Morcelle, S. A. Trejo, F. X. Aviles and N. S. Priolo

Affiliation:

Keywords: Plant proteinases, Asclepiadaceae, Araujia angustifolia, peptide mass fingerprint, proteomics techniques

Abstract: Two cysteine endopeptidases from latex of Araujia angustifolia (araujiain aI and araujiain aIII) were purified and characterized by means of conventional and proteomics techniques (MALDI-TOF). N-terminal sequences showed a high percentage of identity with cysteine proteinases belonging to the papain family. The peptide mass fingerprint analysis demonstrated a close homology among both proteinases.

Cite this article as:

Obregon D. W., Liggieri S. C., Morcelle R. S., Trejo A. S., Aviles X. F. and Priolo S. N., Biochemical and PMF MALDI-TOF Analyses of Two Novel Papain-Like Plant Proteinases, Protein & Peptide Letters 2009; 16 (11) . https://dx.doi.org/10.2174/092986609789353736

DOI https://dx.doi.org/10.2174/092986609789353736	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305