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- 11S11 S
- 11S/7S11S / 7S
- 11S组分7S
- 7S和11S7S and 11 S
- 802.11s802.11 s
- 11S球蛋白11S globulin
- 11S蛋白质11S protein
- 11S/7S比值11 S/ 7S ratio
- 11S和7S组分11S and 7S fraction
- Ca结合11S蛋白11 S Calcium- binding protein
- 11S球蛋白基因11S glycinin gene
- 大豆11S球蛋白soy 11 S globulin
- 钙结合11S大豆蛋白11S Ca-binding protein
- 11S球蛋白Gy7全基因11S glycinin Gy7 gene
- 11S球蛋白Gy7cDNA序列11S glycinin Gy7 cDNA
- 富含11S组分大豆分离蛋白11S--rich soybean protein isolate
- 同时,TG催化MPI与SPI交联在进样端产生1条深色电泳条带(大豆蛋白中除了基本亚基外的7S和11S两亚基)。a reduced intensity in the electrophoretic bands of soy proteins (7S and 11S except the basic subunits) was observed in all treatments, suggesting cross-linking with MPI.
- 氨基酸分析表明,CPI含有人体所需的各种必需氨基酸,计算出CPI及其主要组分11S和7S的平均疏水性分别为4.4、4.05和4.65 KJ/mol氨基酸残基。The average hydrophobicity of CPI, 11S and 7S were 4.4, 4.05 and 4.65 KJ/mol amino acid residues. Hydrophobicity probe (ANS) and differential scanning calorimetry (DSC) were used to determine the surface hydrophobicity (So) and thermal denaturation temperature (Td) of CPI, 11S and 7S.
- SDS-PAGE结果表明,生大豆主要蛋白质成分集中于11S二峰和7S一峰处,熟大豆7S二峰电泳带与生大豆7S带相差不大,说明热处理对其破坏程度较小。The results of SDS-PAGE showed that the major proteins in raw soybeans concentrated at the second peak of 11S and the first peak of 7S globulins,while the profile of the second peak of processed 7S globulin (lane8) has little difference with that of the raw 7S globulin, to which steam-process did little harm.
- SDS-PAGE表明,组分B的亚基相对分子质量为45、38.6、35、20.1和14.4kDa,组分D的亚基相对分子质量为60、55、51、38.6和35 kDa,初步判定这两个组分依次为11S和7S球蛋白。The subunit molecular weights of 45, 38.6, 35, 20.1 andl4.4 kDa for B and 60, 55, 51, 38.6 and 35 kDa for D were obtained by SDS-PAGE. The two major fractions B and D were determined to be 11S and 7S, respectively. Amino acid analysis indicated that CPI contained all essential amino acids.