3
views
0
recommends
+1 Recommend
1 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Comportamiento de glicinina, beta-conglicinina y alfa-amilasa en semillas de soja deterioradas y no deterioradas Translated title: Glycinin, beta-conglycinin and alpha-amylase behaviour in artificially deteriorated and not deteriorated soybean

      research-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          El objetivo del trabajo fue estudiar el comportamiento de glicinina y beta-conglicinina y la actividad de alfa-amilasa en semillas deterioradas y no deterioradas de 10 cultivares de soja [Glycine max (L.) Merr.]. Las semillas se sometieron a dos tratamientos: deterioradas por envejecimiento acelerado y no deterioradas. Se determinó la presencia de las proteínas de reserva a partir de semillas con 0, 3 y 8 días de germinadas por electroforesis en geles de poliacrilamida (SDS-PAGE). La actividad de la alfa-amilasa se determinó bioquímicamente en semillas con 0, 3, 8 y 12 días de germinadas. No hubo diferencias en la presencia de bandas de glicinina y beta-conglicinina en semillas no deterioradas hasta los 8 días de germinadas. Las semillas deterioradas se comportaron en forma similar a las no deterioradas. La actividad de la alfa-amilasa aumentó en semillas germinadas hasta 8 días y disminuyó a los 12 días. En semillas deterioradas la actividad enzimática disminuyó con respecto a las no deterioradas. El deterioro artificial no afectó la presencia de glicinina y beta-conglicinina pero alteró la actividad de la alfa-amilasa hasta los 12 días de germinación. Los cultivares estudiados mostraron comportamiento diferencial frente a la actividad de esta enzima.

          Translated abstract

          The objective of this research was to study the behaviour of the storage proteins glycinin and beta-conglycinin and the alpha-amylase activity in artificially deteriorated and not deteriorated soybean [Glycine max (L.) Merr.] seeds of 10 cultivars. The seeds were submitted to two treatments: deteriorated by accelerated aging and not deteriorated seeds. The presence of glycinin and beta-conglycinin were determined in seeds with 0, 3 and 8 days of germination using polyacrylamid gel electrophoresis (SDS-PAGE). The alpha-amylase activity was biochemically determined in seeds with 0, 3, 8 and 12 days of germination. There were no differences in the presence of glycinin and beta-conglycinin electrophoretic bands in not deteriorated seeds until 8 days of germination. The deteriorated seeds showed a similar behaviour to the not deteriorated seeds. The alpha-amylase activity increased in seeds until the eighth day of germination and decreased to the twelfth day. The enzymatic activity of the deteriorated seeds decreased with respect to that not deteriorated. The artificially deterioration did not affect the presence of glycinin and beta-conglycinin but modified the alpha-amylase activity until the twelfth day of germination. The studied cultivars showed a differential behaviour to the activity of this enzyme.

          Related collections

          Most cited references26

          • Record: found
          • Abstract: not found
          • Article: not found

          Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Effect of phosphorus and zinc nutrition on soybean seed phytic Acid and zinc.

            The relationships between nutrient P and Zn levels and the phytic acid, P, and Zn concentrations in soybean (Glycine max L. Merr. cv ;Williams 79') seed were studied. Phytic acid increased linearly from 4.2 to 19.2 milligrams per gram as nutrient P treatment was varied from 2.0 to 50 milligrams per liter and Zn was held constant at 0.05 milligrams per liter. Leaf P concentration during seed development was found to be closely related to the concentrations of seed P and phytic acid. Leaf and seed Zn concentrations both responded positively to increasing nutrient Zn treatment. The effects of P treatment on plant and seed P and phytic acid were largely independent of the effects of Zn treatment on leaf and seed Zn. Phytic acid to Zn molar ratios ranging from 3.6 to 33.8 were observed.The effects of nutrient P treatments on the concentrations of phytic acid, seed P, and leaf P were also studied in the P-sensitive (gene np) cultivars ;Harosoy' and ;Clark' and their respective P-tolerant (gene Np) near-isogenic lines L66-704 and L63-1677. In general, the positive relationships observed among nutrient P, leaf P, seed P, and phytic acid concentrations were similar to those observed in the studies with Williams 79. When fertilized with low or moderate nutrient P (2.5 and 25.0 milligrams P per liter, respectively) no significant differences in any parameter were observed between Harosoy or Clark and their respective P-tolerant isolines. When fertilized with high nutrient P (100 milligrams P per liter), Harosoy seed had a significantly higher concentration of phytic acid (30 milligrams per gram) than did seed of its P-tolerant near-isogenic line L66-704 (24.2 milligrams per gram phytic acid), whereas no significant difference was observed between Clark and its P-tolerant near-isogenic line L63-1677 (22.8 and 21.6 milligrams per gram, respectively). Variation in the phytic acid concentrations in the mature seed of the cultivars and isolines more closely paralleled leaf P concentrations observed during seed development (49 days after flowering), than those observed at the onset of seed development (14 days after flowering). Electrophoresis and ion-exchange chromatography revealed that partially phosphorylated intermediates do not appear when phytic acid accumulation is greatly reduced by limiting the nutrient P or when accumulation is greatly accelerated by excess P.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Characterization of the Major Protease Involved in the Soybean beta-Conglycinin Storage Protein Mobilization.

              Protease C1, the protease responsible for the initial degradation of the alpha' and alpha subunits of the soybean beta-conglycinin storage protein (Glycine max [L.] Merrill), has been purified. The enzyme was found by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to have a molecular weight of 70,000 and a pH optimum of 3.5 to 4.5. Susceptibility to protease inhibitors indicates that protease C1 is a serine protease. Study of the proteolytic intermediates generated suggests that the cleavage of the alpha' and alpha subunits of beta-conglycinin by protease C1 results in intermediates that are 1 or 2 kilodaltons smaller than the native alpha' and alpha subunits. Following that, a succession of intermediates exhibiting molecular masses of 70.0 and 58.0 kilodaltons, then 63.0, 61.0, 55.0, and 53.5 kilodaltons, are observed. A 50.0- and a 48.0- kilodalton intermediate are the final products of protease C1 action. Comparison of these intermediates with the prominent anti-beta-conglycinin cross-reacting bands that increase during the first few days of germination and early growth show that protease C1 plays an important physiological role, but not an exclusive one, in the living plant.
                Bookmark

                Author and article information

                Journal
                pab
                Pesquisa Agropecuária Brasileira
                Pesq. agropec. bras.
                Embrapa Secretaria de Pesquisa e Desenvolvimento; Pesquisa Agropecuária Brasileira (Brasília, DF, Brazil )
                0100-204X
                1678-3921
                August 2002
                : 37
                : 8
                : 1175-1181
                Affiliations
                [01] Santa Fe orgnameUniversidad Nacional de Rosario orgdiv1Faculdad de Ciencias Agrarias Argentina
                [02] Santa Fe orgnameInstituto Nacional de Tecnología Agropecuaria orgdiv1Estación Experimental Agropecuaria Argentina
                Article
                S0100-204X2002000800016 S0100-204X(02)03700816
                af26f5f5-4197-4370-a9c7-03ae703396fe

                This work is licensed under a Creative Commons Attribution 4.0 International License.

                History
                : 12 September 2001
                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 27, Pages: 7
                Product

                SciELO Brazil

                Self URI: Texto completo solamente en formato PDF (ES)

                storage proteins,enzymic activity,deterioro,proteínas de reserva,electroforesis,germinación,Glycine max,deterioration,electrophoresis,germination,actividad enzimática

                Comments

                Comment on this article