Glycinin
Mostrando 13-24 de 25 artigos, teses e dissertações.
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13. Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer
Most plant seeds contain 11S globulins as major storage proteins for their nutrition. Soybean glycinin belongs to the 11S globulin family and consists of five kinds of subunits. We determined the crystal structure of a homohexamer of the glycinin A3B4 subunit at 2.1-Å resolution. The crystal structure shows that the hexamer has 32-point group symmetry f
National Academy of Sciences.
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14. Survey of the Proteolytic Activities Degrading the Kunitz Trypsin Inhibitor and Glycinin in Germinating Soybeans (Glycine max) 1
The cotyledons of the soybean (Glycine max [L.] Merrill cv Amsoy 71) were examined for proteolytic activities capable of degrading soybean seed proteins. Three distinct activities were identified that attack the native Kunitz soybean trypsin inhibitor of Amsoy 71, Tia. Protease K1 cleaves Tia to Tiam, the inhibitor form lacking the five carboxyl-terminal ami
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15. The glycinin Gy1 gene from soybean.
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16. The glycinin Gy2 gene from soybean.
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17. The glycinin Gy3 gene from soybean.
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18. Inheritance and Organization of Glycinin Genes in Soybean.
Five genes (Gy1, through Gy5) encode most of the subunits that are assembled into glycinin, a predominant seed storage protein found in soybeans. Restriction fragment length polymorphisms are described that identify four of these five genes (Gy1/Gy2, Gy3, and Gy5). The fifth gene (Gy4) is characterized by two alleles, one of which (gy4) causes absence of the
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19. Effect of structural modifications on the assembly of a glycinin subunit.
A Gy4 glycinin cDNA was modified and used to produce structurally altered 11S storage protein subunits. We evaluated these modified subunits for their ability to assemble into oligomers. Alterations made in the acidic polypeptide changed the subunit solubility characteristics but did not eliminate assembly. Modifications in the basic polypeptide usually elim
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20. The glycinin A3B4 mRNA from wild soybean Glycine soja Sieb. et ZUCC.
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21. Complete nucleotide sequence of the gene encoding a glycinin A2B1a subunit precursor of soybean.
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22. Cosuppression of the α Subunits of β-Conglycinin in Transgenic Soybean Seeds Induces the Formation of Endoplasmic Reticulum–Derived Protein Bodies
The expression of the α and α′ subunits of β-conglycinin was suppressed by sequence-mediated gene silencing in transgenic soybean seed. The resulting seeds had similar total oil and protein content and ratio compared with the parent line. The decrease in β-conglycinin protein was apparently compensated by an increased accumulation of glycinin. In addit
American Society of Plant Physiologists.
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23. A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean
The assembly of 11S globulin seed storage proteins in plants is regulated in part by the activity of a protease that cleaves between asparagine and glycine residues. Post-translational cleavage of subunit precursors into acidic and basic polypeptides is associated with the ability of subunits in trimers to aggregate into hexamers in vitro. An activity is pre
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24. Self-assembly of proglycinin and hybrid proglycinin synthesized in vitro from cDNA
An in vitro system was developed that results in the self-assembly of subunit precursors into complexes that resemble those found naturally in the endoplasmic reticulum. Subunits of glycinin, the predominant seed protein of soybeans, were synthesized from modified cDNAs using a combination of the SP6 transcription and the rabbit reticulocyte translation syst