Key result
C-terminal decahistidine tagging of human prorenin enables efficient purification without altering folding or catalytic activity.
A decahistidine tag at the C-terminus allows for efficient purification of recombinant human (pro)renin without compromising its folding or enzymatic activity.
Simplifies recombinant human prorenin production; extends tagging methods but leaves open translation beyond preclinical models.
Human prorenin attached by a decahistidine tag at the C-terminus was produced in Chinese hamster ovary cells. The tagged protein secreted into the culture medium was in the inactive prorenin form, and was activated to mature renin by proteolytic removal of its prosegment by trypsin in the same manner as native prorenin. The tagged (pro)renin was efficiently purified by metal-chelate affinity chromatography. The enzymatic properties of mature renin carrying the tag were similar to native renin. These results indicate that the introduction of a decahistidine tag at the C-terminus does not interfere with either the correct folding of prorenin or the catalytic activity of mature renin.
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Nakagawa et al. (2007) studied this question. Decahistidine tag attached at the C-terminus of human prorenin vs. Native renin was evaluated on Production, activation, purification, and enzymatic properties. Introduction of a decahistidine tag at the C-terminus of human prorenin allowed efficient purification and did not interfere with correct folding or catalytic activity of mature renin.
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