Publications by authors named "Mutsumi Futatsumori-Sugai"

Human interleukin-11 (hIL-11) is a pleiotropic cytokine administered to patients with low platelet counts. From a structural point of view hIL-11 belongs to the long-helix cytokine superfamily, which is characterized by a conserved core motif consisting of four α-helices. We have investigated the region of hIL-11 that does not belong to the α-helical bundle motif, and that for the purpose of brevity we have termed "non-core region.

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Almost all secretory proteins have a sequence consisting of 15-30 amino acids at the N-terminus (the so-called N-terminal signal peptide). Signal peptides direct the propeptide to the endoplasmic reticulum and through the secretory pathway. Although the sequences of signal peptides vary greatly, all contain a basic amino acid in the N-terminal region, followed by a hydrophobic core region.

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Article Synopsis
  • The study tested various conditions for using MEP HyperCel chromatography with two types of conditioned media that contained humanized IgG1 antibodies and bovine serum albumin (BSA).
  • While the antibodies bound to the MEP column without any pre-treatment, many contaminating proteins from the media also bound, indicating they share similar binding characteristics.
  • Ethylene glycol and arginine were effective for eluting the bound proteins, with the MEP resin showcasing selectivity for removing BSA but not for Fc-fusion proteins derived from silkworm larvae, which were hindered by competing serum proteins.
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FLAG-tag is one of the commonly used purification technologies for recombinant proteins. An antibody, M2, specifically binds to the FLAG-tag whether it is attached to N- or C-terminus of proteins to be purified. The bound proteins are generally eluted by competition with a large excess of free FLAG peptide.

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