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J. Biochem, 1996, Vol. 120, No. 2 229-232
© 1996 Japanese Biochemical Society

other

Construction and Expression of Bi-Functional Proteins of Single-Chain Fv With Effector Domains1

Dong Luo*,2, Nancy Mah*, David Wishart{dagger}, Yi Zhang*, Fred Jacobs* and Luis Martin*

*Research and Development Division, Biomira Inc., 2011-94 Street Edmonton, Alberta, Canada
{dagger}Protein Engineering, Department of Biochemistry, University of Alberta Edmonton, Alberta, Canada

2To whom Correspondence should be addressed at the present address: Biotechnology Research and Development, Alta Rex Inc., 1134 Dentistry-Pharmacy, University of Alberta, Edmonton, Alberta, Canada T6G 2N8. Tel: +1-403-492-3197, Fax: +1-403-492-6773

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 minetic sequence. These bi-functional proteins were expressed and secreted in a determined by competitve 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.

1This study was supported by Biomira Inc.


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