Construction and Expression of Bi-Functional Proteins of Single-Chain Fv with Effector Domains.

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概要

• 論文の詳細を見る

• We fused various polypeptide extensions to the C-termini of single chain Fv (scFv) and disulfide-stabilized Fv (dsFv) fragments to facilitate detection of bi-functional proteins or to add biological effector domains, which included the human metallothionein (HMT) motif and biotin mimetic sequence. These bi-functional proteins were expressed and secreted in a recombinant Pichia pastoris system and showed specific anti-idiotype binding activity, as determined by competitive radioimmunoassaying. However, the fusion protein constructed with dsFv- HMT, but not scFv-HMT, had lost this binding activity. The interruption of the structural conformation as a result in dsFv-HMT may be explained by the interactions between the cysteines engineered in dsFv domains and the cysteines in the HMT region.

• 社団法人 日本生化学会の論文

著者

• WISHART David

  Protein Engineering, Department of Biochemistr, University of Alberta

• Zhang Yi

  Research And Development Division Biomira Inc.

• Jacobs Fred

  Research And Development Division Biomira Inc.

• Mah Nancy

  Research And Development Division Biomira Inc.

• Luo Dong

  Research And Development Division Biomira Inc.

• Mah Nancy

  Research and Development Division, Biomira Inc.

• Martin Luis

  Protein Engineering, Department of Biochemistry, University of Alberta

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