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  • Title: Purification and biochemical characterization of 11S globulin from chan (Hyptis suaveolens L. Poit) seeds.
    Author: Bojórquez-Velázquez E, Lino-López GJ, Huerta-Ocampo JA, Barrera-Pacheco A, Barba de la Rosa AP, Moreno A, Mancilla-Margalli NA, Osuna-Castro JA.
    Journal: Food Chem; 2016 Feb 01; 192():203-11. PubMed ID: 26304339.
    Abstract:
    Chan (Hyptis suaveolens) is a Mesoamerican crop highly appreciated since the pre-Hispanic cultures. Its proteins are a good source of essential amino acids; however, there are no reports on the properties of its individual proteins. In this study, the 11S globulin (Hs11S) was purified and biochemically characterized. The molecular weight of native Hs11S was about 150-300 kDa with isoelectric points of 5.0-5.3, composed by four monomers of 53.5, 52, 51.1 and 49.5 kDa, each formed by one acidic subunit and one basic subunit linked by a disulfide bond. Dynamic light scattering, size exclusion chromatography and native PAGE show that Hs11S is assembled in different oligomeric forms. LC-MS/MS analysis confirmed its identity. Hs11S presents antigenic determinants in common with lupin 11S globulin. Carbohydrate moieties or phosphate groups linked to Hs11S were not detected. This information is very useful in order to exploit and utilize rationally chan 11S globulin in food systems.
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