Comparison of C-S Lyase in<i>Lentinus edodes</i>and<i>Allium sativum</i>

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  • KUMAGAI Hitomi
    <i>Department of Agricultural and Biological Chemistry, College of Bioresource Sciences, Nihon University</i>
  • KONO Hidetoshi
    <i>Department of Agricultural and Biological Chemistry, College of Bioresource Sciences, Nihon University</i>
  • SAKURAI Hidetoshi
    <i>Department of Agricultural and Biological Chemistry, College of Bioresource Sciences, Nihon University</i>
  • TOKIMOTO Keisuke
    <i>The Tottori Mycological Institute</i>

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  • Comparison of C-S Lyase in Lentinus edodes and Allium sativum.

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  The characteristics of C-S lyase in Lentinus edodes (shiitake) were compared with those in Allium sativum (garlic). C-S lyase mRNA from shiitake was hybridized with the garlic C-S lyase cDNA fragment, being almost the same length as that from garlic. The isoelectric point of the C-S lyase from shiitake was between pH 4 and 5, while that from garlic was over a wider range between pH 4 and 8. Different from the C-S lyase from garlic, that from shiitake was not a glycoprotein without being stained by PAS, and was not bound to the anti-garlic C-S lyase antibody. Similar to garlic C-S lyase, shiitake C-S lyase comprised a homodimer, and its molecular mass was 84 kDa. However, the N-terminal amino acid sequences of each subunit of shiitake C-S lyase were totally different from those of garlic C-S lyase.<br>

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