dc.creatorLlerena Suster, Carlos Rafael
dc.creatorObregón, Walter David
dc.creatorTrejo, Sebastián Alejandro
dc.creatorMorcelle del Valle, Susana Raquel
dc.date2011
dc.date2020-03-30T18:15:57Z
dc.date.accessioned2023-07-14T19:06:07Z
dc.date.available2023-07-14T19:06:07Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/92371
dc.identifierissn:1532-236X
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7433997
dc.descriptionPapain was purified from dried Carica papaya latex by fractioned salt precipitation in presence of sodium tetrathionate to preserve enzymatic activity. Purification was followed by different electrophoretic methods. Identification of the purified product was afforded by submitting the peptides obtained by tryptic digestion of papain to matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF/TOF MS) analysis. Comparison of the peptide masses analyzed by peptide mass fingerprinting (PMF) MALDI-TOF and those obtained by theoretical tryptic digestion, revealed the presence of some peptides belonging the other three endopeptidases contained in papaya latex (very similar to papain in molecular weight and pI) in the purified fraction of papain. The PMF by MALDI-TOF could be applied as a method to follow papain purification.
dc.descriptionCentro de Investigación de Proteínas Vegetales
dc.formatapplication/pdf
dc.format2124-2137
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.rightsCreative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.subjectBiología
dc.subjectCaricain
dc.subjectChymopapain
dc.subjectGlycyl endopeptidase
dc.subjectMALDI-TOF
dc.subjectPeptide mass fingerprint
dc.subjectPapain
dc.titlePapain purification insights: monitoring by electrophoretic approaches and MALDI-TOF peptide mass fingerprint analyses
dc.typeArticulo
dc.typeArticulo


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