Cloning and Expression of the C-Terminal Lobe of Human Lactoferrin
Three dimensional studies of human lactoferrin (Anderson et al, 1989) have shown that like all other members of the transferrin family, lactoferrin is divided into two lobes; the N-terminal and the C-terminal lobes. Each lobe is capable of synergistically binding one Fe3+ ion and one anion. The cloning of the cDNA for human lactoferrin (hLf) and its subsequent expression in mammalian cells (Stowell et al, 1991) has provided an excellent system to probe the structure and function of hLf by site-directed mutagenesis. The first mutant to be cloned and expressed using this system was the N-terminal lobe (LfN) of hLf (Day et al, 1992). Recombinant protein concentrations of up to 30 mg/1 in the tissue culture medium have been obtained.
KeywordsSignal Peptide Sequence Signal Peptidase Baby Hamster Kidney Cell Human Lactoferrin Dimensional Study
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