Expression and characterization of a mutant recombinant blood coagulation factor VIII (rFVIII (m))

Abstract

In an earlier study, a site directed mutant rFVIII (rFVIII m and native FVIII with APC decreased their cofactor activities, however, the former exhibited a slower decrease than the latter, although no significant difference was present. rFVIII m formed a complex with vWF, resulting in a stabilized form, and the lag period of thrombin-mediated activating was extended by vWF association. These results implicated that rFVIII m expressed in baculovirus-insect cell system had a comparable capacity as FVIII cofactor activity and might be a good candidate for the FVIII replacement therapy for hemophilia A patients.

Evidence that the fully assembled capsid of Leishmania RNA virus 1-4 possesses catalytically active endoribonuclease activity

“…The three point mutants of LRV1-4 capsid carrying substitutions in the N-terminal half (P1, P2, and P3) were generated by using PCR-direct mutagenesis as previously described (Oh et al, 2002) and the primers listed in Table 1. Briefly, for the construction of mutant P1 which contains a substitution of Cys-47 residue to Ser (C47S), a primer (P1-L) containing a mismatch at nt 140 (G to C) and polyhedrin reverse sequencing primer (Ph-Rev, Invitrogen) were used to prime a DNA fragment synthesis from pTCB2 as a template.…”