We isolated cDNA clones coding for the functionally important tryptic N-terminal38-
kDa fragment of human complement control protein factor H using polyclonal and
monoclonal antibodies to screen a human liver cDNA library cloned in a bacterial
expression vector, PEX-1. By testing the reactivity of antibodies specific for the
recombinant proteins produced by individual clones with proteolytic fragments of
serum H the exact position of these cDNA clones within H was mapped. One clone,
H-19, coding for the 38-kDa fragment of H was sequenced and found to code for 289
amino acids derived from the 38-kDa N-terminal fragment as well as for the first 108
amino acids belonging to the complementary 142-kDa tryptic fragment. The derived
protein sequence could be arranged in 6 highly homologous repeats of about 60 amino
acids each, the homology between the repeats being determined by the characteristic
position of cysteine, proline, glycine, tyrosine and tryptophane residues. The region
coding for the epitope recognized by one of our monoclonal antibodies was localized
by subcloning restriction fragments of H-19 into the expression plasmid and testing
for the expression of this epitope
