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Commentary
Reference
expression and partial characterization of soluble recombinant PM I from Plasmodium falciparum in which a truncated form of PM I (Lys77P-Leu329) (P indicates a propart residues) is fused to thioredoxin in the pET32b(1) vector, Trx-tPM I and expressed in Escherichia coli Rosetta-gami B (DE3)pLysS. The soluble fusion protein is purified from cell culture using a combination of Ni21 affinity and gel filtration chromatography and is capable of autocatalytic activation at pH 4.0–5.5, which occurrs at Leu116P-Ser117P, seven residues upstream of the native cleavage site (Gly123P-Asn1)
expression in Escherichia coli
expression of proplasmepsin I and V110P-proplasmepsin in Escherichia coli; initial attempts to express full-length proplasmepsin I gene in Escherichia coli results in very low expression levels, possibly due to the toxic effects of the hydrophobic segment, and no activation to mature plasmepsin I is ever observed. Recombinant proplasmepsin I is expressed from pETPMI, a construct that is prepared from pET3a and contains the last 48 residues of the propart followed by the 328 residues of mature plasmepsin I. It is necessary to introduce a processing site, V110P, into the zymogen that renders the precursor capable of undergoing autoactivation
expression of truncated proPfPM1 K110pN mutant in Escherichia coli
Results 1 - 5 of 5