W. D. Obregon, C. S. Liggieri, S. R. Morcelle, S. A. Trejo, F. X. Aviles and N. S. Priolo Pages 1323 - 1333 ( 11 )
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.
Plant proteinases, Asclepiadaceae, Araujia angustifolia, peptide mass fingerprint, proteomics techniques
LIPROVE, Depto. Cs. Biologicas, Fac. Cs. Exactas, UNLP. Calles 47 y 115, La Plata (1900), Argentina.