Abstract
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. © 1999 by Japan Society for Bioscience, Biotechnology, and Agrochemistry.
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Kumagai, H., Kono, H., Sakurai, H., & Tokimoto, K. (2002). Comparison of C-S lyase in lentinus edodes and alliu. Bioscience, Biotechnology and Biochemistry, 66(12), 2560–2566. https://doi.org/10.1271/bbb.66.2560
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