Biochemical and PMF MALDI-TOF analyses of two novel papain-like plant proteinases.
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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Laboratorio 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
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D029062:Apocynaceae / Q000201:enzymology*; D019295:Computational Biology / Q000379:methods; D057056:Cysteine Proteases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry; D004952:Esters / Q000378:metabolism; D005638:Fruit / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007840:Latex / Q000737:chemistry; D010206:Papain / Q000737:chemistry* / Q000378:metabolism; D010449:Peptide Mapping / Q000379:methods*; D010940:Plant Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
D015853:Cysteine Proteinase Inhibitors; D004952:Esters; D007840:Latex; D010940:Plant Proteins; D057056:Cysteine Proteases; D010206:Papain