Structure-physicochemical function relationships of soybean beta-conglycinin constituent subunits.

@article{Maruyama1999StructurephysicochemicalFR,
  title={Structure-physicochemical function relationships of soybean beta-conglycinin constituent subunits.},
  author={Nobuyuki Maruyama and Ryoko Sato and Yusuke Wada and Yasuki Matsumura and Hitomi Goto and Eiko Okuda and Shuko Nakagawa and Syunsaku Utsumi},
  journal={Journal of agricultural and food chemistry},
  year={1999},
  volume={47 12},
  pages={5278-84}
}
Beta-conglycinin, one of the dominant storage proteins of soybean, has a trimeric structure, being composed of three subunits alpha, alpha', and beta. The alpha and alpha' subunits contain the extension regions in addition to the core regions common to all subunits, which are N-glycosylated. Physicochemical functions of recombinant nonglycosylated individual subunits and deletion mutants (alpha(c) and alpha'(c)) lacking the extension regions of the alpha and alpha' subunits were examined at pH… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 12 extracted citations

Similar Papers

Loading similar papers…