dc.creatorBruno, Mariela Anahí
dc.creatorPardo, Marcelo Fabián
dc.creatorCaffini, Néstor Oscar
dc.creatorLópez, Laura María Isabel
dc.date2003
dc.date2022-08-31T14:38:45Z
dc.date.accessioned2023-07-15T04:49:12Z
dc.date.available2023-07-15T04:49:12Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/141355
dc.identifierissn:0277-8033
dc.identifierissn:1573-4943
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7471005
dc.descriptionA new peptidase, named hieronymain I, was purified to homogeneity from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae) by acetone fractionation followed by cation exchange chromatography (FPLC) on CM-Sepharose FF. Homogeneity of the enzyme was confirmed by mass spectroscopy (MALDI-TOF), isoelectric focusing, and SDS-PAGE. Hieronymain is a basic peptidase (pI > 9.3) and its molecular mass was 24,066 Da. Maximum proteolytic activity on casein (>90% of maximum activity) was achieved at pH 8.5-9.5. The enzyme was completely inhibited by E-64 and iodoacetic acid and activated by the addition of cysteine; these results strongly suggest that the isolated protease should be included within the cysteine group. The N-terminal sequence of hieronymain (ALPESIDWRAKGAVTEVKRQDG) was compared with 25 plant cysteine proteases that showed more than 50% of identity.
dc.descriptionCentro de Investigación de Proteínas Vegetales
dc.formatapplication/pdf
dc.format127-134
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.subjectBromelia hieronymi
dc.subjectBromeliaceae
dc.subjectplant peptidases
dc.subjectcysteine proteinase
dc.titleHieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae)
dc.typeArticulo
dc.typeArticulo


Este ítem pertenece a la siguiente institución