Utilize este identificador para referenciar este registo: http://hdl.handle.net/10451/20919
Título: Characterization of globulins from common vetch (Vicia sativa L.)
Autor: Ribeiro, AC
Teixeira, AR
Ferreira, RB
Palavras-chave: Agriculture, Multidisciplinary
Chemistry, Applied
Food Science & Technology
Data: 2004
Citação: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. - Vol. 52, n. 15 (2004), p. 4913-4920
Resumo: The proteins from Vicia sativa L. (common vetch) seeds were investigated. Protein comprises similar to11.4% of the seed fresh weight, 50.8% of which is composed by globulins and 43.6% by albumins. The globulins may be fractionated into two main components, which were named alpha-vicinin (comprising 73% of the total globulin fraction, and hence 37% of the total seed protein) and beta-vicinin. Two minor globulin components are also present, gamma-vicinin and delta-vicinin. alpha-Vicinin, the legumin-like globulin, with a sedimentation coefficient of 10.6 S, is a nonglycosylated, disulfide-bond-containing globulin, composed of a group of subunits with molecular masses ranging from 50 to 78 kDa. Upon reduction, each of these subunits releases a heavy polypeptide chain, (34-66 kDa) and a light polypeptide chain (21-23 kDa). beta-Vicinin, the vicilin-like globulin, with a sedimentation coefficient of 7.7 S, is a nonglycosylated globulin that contains no disulfide bonds and consists of two major polypeptides with molecular masses of 58 and 66 kDa. gamma-Vicinin is a minor, glycosylated, disulfide-bond-containing globulin. In the reduced form, it comprises six polypeptide chains with molecular masses of 12, 19, 21, 22, 23, and 31 kDa. Finally, delta-vicinin is a minor, highly glycosylated globulin that exhibits hemagglutinating activity. It is composed of a major 47 kDa polypeptide and two minor (33 and 38 kDa) polypeptides. N-terminal sequencing of the delta-vicinin 47 kDa polypeptide revealed no homology to any other known storage protein.
URI: http://hdl.handle.net/10451/20919
DOI: http://dx.doi.org/10.1021/jf049833p
ISSN: 0021-8561
Aparece nas colecções:FF - Produção Científica 2000-2009

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