Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/99045
Type: Artigo de periódico
Title: Characterization Of The Storage Protein In Seed Of Coix Lacryma-jobi Var. Adlay
Author: Ottoboni L.M.M.
Leite A.
Targon M.L.N.
Crozier A.
Arruda P.
Abstract: The endosperm of seed of Coix lacryma-jobi var. Adlay contains ca. 20% protein distributed between fraction 1 (albumins and globulins), fraction 2 (prolamins), and fraction 3 (residual proteins) extracts. The major component is prolamin, known as coixin, the amount of which ranged from 8.4% to 78.7% of the total endosperm protein depending upon the concentration of 2-mercaptoethanol in the extraction solvent. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis separated coixin into five components with molecular weights of 27K (C1), 25K (C2), 22K (C3), 17.5K (C4), and 15K (C5). Isoelectric focusing (IEF) of coixin resolved seven major protein bands. Analysis of the individual IEF bands by SDS-PAGE and immunoblotting, using rabbit antibodies raised against C2 and C3, indicated an even greater complexity, with a total of 17 proteins being detected. Amino acid analysis revealed that protein fractions from Coix endosperm have the typical composition of Panicoideae endosperm. The predominant fraction, coixin, is rich in proline and leucine and poor in lysine. © 1990 American Chemical Society.
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Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-4644351701&partnerID=40&md5=d1d4a4b1497a3b353968c637dd0b1fe5
Date Issue: 1990
Appears in Collections:Unicamp - Artigos e Outros Documentos

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