Evidence for accumulation of the β-subunit of β-conglycinin in soybean [Glycine max (L) Merr.] embryonic axes

Abstract

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of total proteins from soybean cotyledons and embryonic axes revealed the presence of similar storage proteins in both organs. Results from Western blot analysis conducted with antibodies raised against the purified β-subunit of β-conglycinin demonstrated accumulation of the β-subunit in embryonic axes. This accumulation followed a temporal pattern similar to that shown by the cotyledons. Axis β-conglycinin was broken down during the initial stage(s) of seed germination and was completely mobilized within 3 days after imbibition. Subcellular fractions were isolated from developing embryonic axes using metrizamide density gradients and analyzed by Western blots. Storage proteins were enriched in the lighter fractions of the gradient as well as with immunoglobulin heavy-chain binding protein. Electron microscopy of the storage-protein-enriched gradient fraction revealed small vesicles and protein aggregates. Protein A-gold immunocytochemistry was used to localize the occurrence of the β-subunit of β-conglycinin within the protein aggregates present in the metrizamide gradient and in the protein bodies present in mature embryonic axes.Evidence for accumulation of the β-subunit of β-conglycinin in soybean [Glycine max (L) Merr.] embryonic axes

Analysis of Soybean Embryonic Axis Proteins by Two-Dimensional Gel Electrophoresis and Mass Spectrometry

“…Ostergaard et al [72] reported the presence of three types of peroxiredoxin in barley seeds, that are proposed to protect the embryo and aleurone against reactive oxygen species and free radicals during seed development and desiccation. In addition, we found nine spots of biotinylated seed protein (spot 27,28,29,31,32,33,34,35,36) in our study. Biotinylated enzymes such as acetyl-CoA carboxylase, 3-methylcrotonoyl-CoA carboxylase, propionylCoA carboxylase and pyruvate carboxylase have been identified in plants.…”

“…Twenty protein spots from our gels were successfully identified as subunits of -conglycinin (19, 20, 23-25, 37, 45, 46, 48, 90, 92, 94, 103, 114, 115, 210, 278, 282, 303, 316). We did not find anysubunit of -conglycinin even though its accumulation was clearly demonstrated in the embryonic axis by immunoblot analysis [27]. Using an immunoprecipitation technique, Meinke et al [1] also reported the absence of this -subunit in the embryonic axis of Glycine max cv.…”

Effects of foliar applications of ascobin on seed protein accumulation in soybean (Glycine max (L.) Merrill) JS 1215 grown under cadmium stress

“…We studied the effect of Cd on soybean major fractions, i.e., the 7S (β-conglycinin) and 11S (glycinin) fractions and it was found that the total yield of glycinin and βconglycinin showed differences with change in concentration of ascobin. According to Krishnan (2002)…”

A Proteomics Approach to Study Soybean and Its Symbiont Bradyrhizobium japonicum –A Review

“…2-DE-MAL-DI-TOF-MS followed by Delta2D image analysis showed huge differences in 11S storage globulins amongst the accessions. In addition, the trait for high protein from PI407788A was moved to experimental line LG99-469 and was stable upon transformation [89,90].…”