Abstract
Animal leguminous-type (L-type) lectins, including ERGIC-53 and VIP36 are responsible for intracellular transport and quality control of N-linked glycoproteins in the early secretory pathway. These lectins possess the carbohydrate recognition domain (CRD), which recognizes high-mannose-type glycans in a Ca2+-dependent manner. Here we describe the procedures involved in bacterial overproduction and purification of the CRDs of the animal L-type lectins.
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Acknowledgements
We thank Dr. Yukiko Kamiya (Nagoya University, Japan) for useful discussion. This work was supported in part by JSPS KAKENHI (Grant Numbers JP19H03361 to T.S.). We thank Drs. Kazuo Yamamoto (The University of Tokyo, Japan) and Hans-Peter Hauri (University of Basel, Switzerland) for providing protein expression systems.
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Satoh, T., Kato, K. (2020). Recombinant Expression and Purification of Animal Intracellular L-Type Lectins. In: Hirabayashi, J. (eds) Lectin Purification and Analysis. Methods in Molecular Biology, vol 2132. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0430-4_3
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DOI: https://doi.org/10.1007/978-1-0716-0430-4_3
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