S
Sandino Estrada-Mondaca
Researcher at Paul Sabatier University
Publications - 12
Citations - 524
Sandino Estrada-Mondaca is an academic researcher from Paul Sabatier University. The author has contributed to research in topics: Active site & Substrate (chemistry). The author has an hindex of 10, co-authored 12 publications receiving 516 citations. Previous affiliations of Sandino Estrada-Mondaca include National Autonomous University of Mexico.
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Journal ArticleDOI
Engineering sensitive acetylcholinesterase for detection of organophosphate and carbamate insecticides.
TL;DR: It appears that insect acetylcholinesterase is more susceptible to a broad range of organophosphates and carbamates insecticides than the other tested enzymes.
Journal ArticleDOI
Acetylcholinesterase engineering for detection of insecticide residues
Yvan Boublik,Pascale Saint-Aguet,Andrée Lougarre,Muriel Arnaud,Francois Villatte,Sandino Estrada-Mondaca,Didier Fournier +6 more
TL;DR: The results highlighted the difficulty of predicting the effect of mutations; this may be due to the structure of the site, a deep gorge with the active serine at the bottom and to allosteric effects between the top and the bottom of the gorge.
Journal ArticleDOI
Differences in the glycosylation profile of a monoclonal antibody produced by hybridomas cultured in serum-supplemented, serum-free or chemically defined media.
J. Antonio Serrato,Vanessa Hernández,Sandino Estrada-Mondaca,Laura A. Palomares,Octavio T. Ramírez +4 more
TL;DR: A desirable decrease in sialylated structures, but an undesirable increase in fucosylated forms, was observed in mAb produced in SFM and CDM media, which can explain the higher G0 content compared with cultures in the other two media.
Book ChapterDOI
Stabilization of Recombinant Drosophila Acetylcholinesterase
TL;DR: Affinity-purified recombinant Drosophila melanogaster acetylcholinesterase proved to be instable, but it is shown that such instability can be counterbalanced by provoking protein-protein interactions, either between enzyme molecules or with other molecules such as bovine serum albumin.
Journal ArticleDOI
Stabilization of RecombinantDrosophilaAcetylcholinesterase
TL;DR: Drosophila melanogasteracetylcholinesterase proved to be instable; an apparent cause of this seemed to be the presence of contaminants with protease activity as evidenced by SDS–PAGE, but such instability can be counterbalanced by provoking protein–protein interactions.