Characterization and cDNA cloning of monomeric lectins that correspond to the B-Chain of a type 2 ribosome-inactivating protein from the bark of Japanese elderberry (Sambucus sieboldiana).

M. Rojo; H. Kaku; N. Ishii-Minami; E. Minami; M. Yato; S. Hisajima; T. Yamaguchi; N. Shibuya

DOI:10.1093/JB/MVH060

Corpus ID: 41872283

Characterization and cDNA cloning of monomeric lectins that correspond to the B-Chain of a type 2 ribosome-inactivating protein from the bark of Japanese elderberry (Sambucus sieboldiana).

@article{Rojo2004CharacterizationAC,
  title={Characterization and cDNA cloning of monomeric lectins that correspond to the B-Chain of a type 2 ribosome-inactivating protein from the bark of Japanese elderberry (Sambucus sieboldiana).},
  author={M. Rojo and H. Kaku and N. Ishii-Minami and E. Minami and M. Yato and S. Hisajima and T. Yamaguchi and N. Shibuya},
  journal={Journal of biochemistry},
  year={2004},
  volume={135 4},
  pages={
          509-16
        }
}

M. Rojo, H. Kaku, +5 authors N. Shibuya

Published 2004

Biology, Medicine

Journal of biochemistry

Two monomeric lectins, SSA-b-3 and SSA-b-4, were purified from the bark tissue of Japanese elderberry, Sambucus sieboldiana. SDS-PAGE of the purified lectins showed the presence of single bands of 35 and 33 kDa for SSA-b-3 and SSA-b-4, respectively, irrespective of the presence of reducing agent. MS analysis as well as gel filtration of these lectins indicated that they exist mostly as monomeric lectins. Analysis of the N-terminal amino acid sequences of SSA-b-3 and SSA-b-4 yielded an identical… CONTINUE READING

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