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. 2004 Jan;135(1):164–172. doi: 10.1111/j.1365-2249.2004.02314.x

Fig. 2.

Fig. 2

(a, b) The amino acid sequences for human PR3 (hPR3), human leucocyte elastase (ELA) and murine PR3 (mPR3) used as templates for the recombinant proteins. The signal peptides and propeptides are removed and a HindIII site is introduced at the 5′ end and a NotI site is introduced at the 3′ end. All the recombinant molecules were mutated at the active site by changing Ser to Gly (shaded) to create enzymatically inactive mutants. The cleavage sites for the different constructs are marked a, b, c and d. (c) The chimeric constructs were named according to the origin of the respective proportions of the molecule, where P stands for hPR3, p for mPR3 and E for elastase. For example the PPp construct is comprised of hPR3 from a to c and the last part, from c to d, is mPR3 and the PEP construct is comprised of hPR3 from a to b, elastase from b to c and hPR3 from c to d. rhPR3 is recombinant hPR3, rmPR3 is recombinant mPR3 and rHLE is recombinant HLE.