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NMR in interaction studies of a serine protease from snake venom

Authors :
Giovanna Grillo
Ljubica Tasic
Roney Vander dos Santos
Source :
Resumos do....
Publication Year :
2019
Publisher :
Universidade Estadual de Campinas, 2019.

Abstract

In this research, we have purified a serine protease from Bothrops jararaca venom (BjSP24). This enzyme showed molar mass of 24.4 kDa as determined using MALDI-TOF. BjSP24 inhibition by hesperitin (Hst) was studied using florescence, enzymatic kinetics and nuclear magnetic resonance techinique (Saturation Transferee Difference, STD-NMR).

Subjects

Subjects :
chemistry.chemical_classification
Serine protease
Molar mass
Bothrops jararaca
biology
Kinetics
Venom
biology.organism_classification
Enzyme
chemistry
Biochemistry
Snake venom
biology.protein
Saturation (chemistry)

Details

Database :
OpenAIRE
Journal :
Resumos do...
Accession number :
edsair.doi...........68461230a10e43e5a0134831438dd9b4
Full Text :
https://doi.org/10.20396/revpibic2720192080
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