Upload resources

Upload your works to SEDICI to increase its visibility and improve its impact

 

Show simple item record

dc.date.accessioned 2023-05-18T15:02:13Z
dc.date.available 2023-05-18T15:02:13Z
dc.date.issued 2013
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/153185
dc.description.abstract The properties of morrenain b II, a proteinase isolated from the latex of Morrenia brachystephana, were compared with those of morrenain o II, a proteinase obtained from the latex of Morrenia odorata. Both peptidases were purified to homogeneity by acetone precipitation followed by cation exchange chromatography. The enzymes have pi values higher than 9.3 and similar molecular masses (close to 26 kDa) as determined by SDS-PAGE. They display maximum proteolytic activity within an alkaline pH range, and also exhibit esterolytic activity. The N-terminal sequences of morrenain o II and morrenain b II show a high degree of homology between each other and to other cysteine plant proteinases. en
dc.language en es
dc.subject Latex peptidases es
dc.subject Morrenain es
dc.subject Protein purification es
dc.subject Thiol peptidases es
dc.title Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae) en
dc.type Articulo es
sedici.identifier.other https://doi.org/10.1515/bchm.2001.382.5.879/html es
sedici.identifier.issn 1437-4315 es
sedici.creator.person Vairo Cavalli, Sandra Elizabeth es
sedici.creator.person Cortadi, Adriana A. es
sedici.creator.person Arribére, María Cecilia es
sedici.creator.person Conforti, Paula Andrea es
sedici.creator.person Caffini, Néstor Oscar es
sedici.creator.person Priolo de Lufrano, Nora Silvia es
sedici.subject.materias Química es
sedici.subject.materias Biología es
sedici.description.fulltext true es
mods.originInfo.place Centro de Investigación de Proteínas Vegetales es
sedici.subtype Articulo es
sedici.rights.license Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
sedici.rights.uri http://creativecommons.org/licenses/by-nc-sa/4.0/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle Biological Chemistry es
sedici.relation.journalVolumeAndIssue vol. 382, no. 5 es


Download Files

This item appears in the following Collection(s)

Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) Except where otherwise noted, this item's license is described as Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)