dc.creatorObregón, Walter David
dc.creatorArribére, María Cecilia
dc.creatorMorcelle del Valle, Susana Raquel
dc.creatorLiggieri, Constanza Silvina
dc.creatorCaffini, Néstor Oscar
dc.creatorPriolo de Lufrano, Nora Silvia
dc.date2001
dc.date2022-10-11T16:59:37Z
dc.date.accessioned2023-07-15T05:12:31Z
dc.date.available2023-07-15T05:12:31Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/143564
dc.identifierissn:0277-8033
dc.identifierissn:1573-4943
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7472491
dc.descriptionTwo new endopeptidases were purified to homogeneity from the latex of Araujia hortorum fruits by a simple purification procedure involving ultracentrifugation and ion exchange chromatography. Molecular weights of araujiain h II and araujiain h III were 23,718 and 23546 (mass spectrometry), respectively. The isoelectric point of araujiain h II was 8.9, whereas araujiain h III had a pI higher than 9.3. Maximum proteolytic activity on caseine was reached at pH 8.0-9.0 for both endopeptidases, which were irreversibly inhibited by iodoacetate and E-64, suggesting they belong to the cysteine protease family. Esterolytic activity was determined on N-alpha-CBZ-amino acid-p-nitrophenyl esters, and the highest kcat/Km values for the both enzymes were obtained with the glutamine derivative. The N-terminal sequences of araujiain h II and araujiain h III showed a high degree of homology with other plant cysteine endopeptidases.
dc.descriptionCentro de Investigación de Proteínas Vegetales
dc.formatapplication/pdf
dc.format317-325
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.subjectQuímica
dc.subjectAraujiain
dc.subjectCysteine endopeptidases
dc.subjectLatex
dc.subjectMilkweed family
dc.subjectProtein purification
dc.titleTwo new cysteine endopeptidases obtained from the latex of Araujia hortorum fruits
dc.typeArticulo
dc.typeArticulo


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