Recombinant proteins representing different fragments of rC1-2 [1-233] were generated by PCR amplification. Cysteines at various positions were replaced by using a primer with a serine codon. Recombinant proteins were either purified or immobilized directly from bacterial lysate and assayed for binding of CD36 as described in Fig 2. Binding is given in semi-quantitative results: +++ high binding; ++ moderate binding; + low binding; ± very low but detectable binding; − zero binding. Mutants rC1-2 [1-179] ser32, rC1-2 [1-179] ser41 and rC1-2 [1-179] ser51 were expressed at very low levels in E coli and could not be assayed effectively. rC1-2 [1-179] alone, containing a six-histidine tag, was expressed in yeast and assayed bound to nickel-agarose resin.