dc.creator | Bruno, Mariela Anahí | |
dc.creator | Pardo, Marcelo Fabián | |
dc.creator | Caffini, Néstor Oscar | |
dc.creator | López, Laura María Isabel | |
dc.date | 2003 | |
dc.date | 2022-08-31T14:38:45Z | |
dc.date.accessioned | 2023-07-15T04:49:12Z | |
dc.date.available | 2023-07-15T04:49:12Z | |
dc.identifier | http://sedici.unlp.edu.ar/handle/10915/141355 | |
dc.identifier | issn:0277-8033 | |
dc.identifier | issn:1573-4943 | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/7471005 | |
dc.description | A 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.description | Centro de Investigación de Proteínas Vegetales | |
dc.format | application/pdf | |
dc.format | 127-134 | |
dc.language | en | |
dc.rights | http://creativecommons.org/licenses/by-nc-sa/4.0/ | |
dc.rights | Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) | |
dc.subject | Biología | |
dc.subject | Bromelia hieronymi | |
dc.subject | Bromeliaceae | |
dc.subject | plant peptidases | |
dc.subject | cysteine proteinase | |
dc.title | Hieronymain I, a New Cysteine Peptidase Isolated from Unripe Fruits of <i>Bromelia hieronymi</i> Mez (Bromeliaceae) | |
dc.type | Articulo | |
dc.type | Articulo | |