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Abstract
Chenopodin is an 11S-type globulin purified from Chenopodium quinoa seeds, which can bind carbohydrates and hemagglutinating human erythrocytes. The present study aimed to evaluate the N-terminal structure of the heterodimeric Chenopodin and its effects in models of inflammation. Chenopodin presented two subunits on its structure and has N-terminal homology with other Chenopodin in 92%. Chenopodin decreased paw edema and neutrophil recruitment induced by carrageenan in mice. Concluding, we demonstrated that Chenopodin exhibits in vivo anti-inflammatory activity.
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Disclosure statement
The authors declare no conflict of interest.
Additional information
Funding
This work was supported by the National Council for Scientific and Technological Development (CNPq) under number 303307/2018-8; and Minas Gerais Research Foundation (FAPEMIG) under number APQ–03120-16. We are grateful to Coordination for the Improvement of Higher Education Personnel (CAPES – Finance code 001).