Synthesis of biologically active deletion mutants of human factor VIII:C.

Abstract

The recent cloning and sequence analysis of human factor VIII:C (antihaemophilic factor) revealed a domain structure for the protein which can be presented as A1-A2-B-A3-C1-C2. In this report we describe the construction of two altered factor VIII:C cDNAs coding for molecules in which a part (amino acids 816 to 1598) or all of the B domain (amino acids 741 to 1689) was removed. In the latter mutant a new thrombin cleavage site has been created, which does not exist in wild-type factor VIII:C. The mutated cDNAs were cloned into eucaryotic expression vectors based on regulatory sequences of the virus SV40 and transfected into two different mammalian cell lines. Both truncated recombinant factor VIII:C molecules were secreted into the culture medium, showed full biological activity and could be activated by thrombin.

Cite this paper

@article{Langner1988SynthesisOB, title={Synthesis of biologically active deletion mutants of human factor VIII:C.}, author={Katrin Langner and R. E. Bird and Russell J. McCandliss and Bettina Huber and Egon P. Amann and Gerd Zettlmeissl and Hans A. K{\"{u}pper}, journal={Behring Institute Mitteilungen}, year={1988}, volume={82}, pages={16-25} }