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Updated: Jun 17, 2026

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes
Published on: May 25, 2018
Biochemical and PMF MALDI-TOF analyses of two novel papain-like plant proteinases
W D Obregón1, C S Liggieri, S R Morcelle
1Laboratorio de Investigación de Proteínas Vegetales (LIPROVE), Depto. Cs. Biológicas, Fac. Cs. Exactas, Universidad Nacional de La Plata, La Plata, Argentina. davidobregon@biol.unlp.edu.ar
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.

