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

W.   D.   Obregon; C.   S.   Liggieri; S.   R.   Morcelle; S.   A.   Trejo; F.   X.   Aviles; N.   S.   Priolo

doi:10.2174/092986609789353736

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.

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

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Protein & Peptide Letters

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

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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.

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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