Sequence and specificity of a soluble lactose-binding lectin from Xenopus laevis skin.

@article{Marschal1992SequenceAS,
  title={Sequence and specificity of a soluble lactose-binding lectin from Xenopus laevis skin.},
  author={Philippe Marschal and Jo{\~a}o Lourenço Herrmann and Hakon Leffler and S H Barondes and Douglas N. W. Cooper},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 18},
  pages={
          12942-9
        }
}
A 16-kDa lactose-binding lectin comprises 5% or more of the soluble protein in Xenopus laevis skin. This lectin is mainly localized in the cytoplasm of granular gland cells. In response to stress, the lectin along with a variety of toxic and antibiotic peptides are released onto the skin surface by holocrine secretion. We have purified the lectin, sequenced tryptic peptides using tandem mass spectrometry and Edman degradation, and isolated full-length cDNA using a deduced oligonucleotide… CONTINUE READING

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