The primary structures and properties of non-stomach lysozymes of sheep and cow, and implication for functional divergence of lysozyme.

@article{Ito1993ThePS,
  title={The primary structures and properties of non-stomach lysozymes of sheep and cow, and implication for functional divergence of lysozyme.},
  author={Yoshitake Ito and Hideo Yamada and Masaya Nakamura and Akikazu Yoshikawa and Takashi Ueda and Toshiaki Imoto},
  journal={European journal of biochemistry},
  year={1993},
  volume={213 2},
  pages={
          649-58
        }
}
Lysozymes were purified from the homogenate of cow and sheep kidneys, and their amino-acid sequences as well as some enzymic properties were determined. Like most mammalian lysozymes both sheep and cow kidney lysozymes are composed of 130 amino acids. The sequences of these two lysozymes are the most similar to each other (95% identity), the second most similar to the conventional mammalian lysozymes like human, rat and rabbit lysozymes (74-85% identity), and much less similar to their own… CONTINUE READING
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