Structural homology among the major 7s globulin subunits of soybean seed storage proteins |
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Institution: | 1. College of Food Science and Engineering, Shaanxi Engineering Research Centre of Dairy Products Quality, Safety and Health, Northwest A&F University, Yangling 712100, China;2. Zhejiang Zhongmengchang Health Technology Co., Ltd., Hangzhou 310000, China;3. Shaanxi Baiyue Youlishi Dairy Industry Co., Ltd., Xianyang 712000, China |
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Abstract: | The soybean seed 7S globulin subunits, i.e. α, α′, β and γ-subunits of β-conglycinin, the γ-conglycinin subunit and the HI/HII and LII subunits of basic 7S globulin were purified and the NH2-terminal amino acid sequences of all these subunits except the γ-subunit of β-conglycinin were determined. Only the NH2-terminal regions of the α and α′-subunits showed high sequence homology. However, sequencing of tryptic peptides from the seven subunits revealed that internal region sequences were highly homologous among the four subunits of β-conglycinin. In contrast to the β-conglycinin subunits, no sequence homology was found among the other subunits. On the basis of these results, the major 7S globulin fraction is considered more heterogeneous in primary structure than another major globulin fraction, 11S globulin (glycinin), in soybean seeds. |
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