PPIasePeptidyl-Prolyl Cis-Trans Isomerase
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To measure PPIase activity, an in vitro colorimetric assay was used on protein extracts from symbiotic A.
Given that the protein extracts contained both algal and host proteins, the PPIase activity could have derived from both host and algal CsA-sensitive constituents.
The PPiase activity of cyclophilins plays a role in the stress response of organisms.
Given that CsA also inhibits in vitro PPIase activity, it is possible that the production of ROS is mediated through alteration of one or more CsA-sensitive PPIase-dependent mechanisms.
pallida was not sensitive to CsA treatment even when incubated at a concentration two orders of magnitude greater than necessary to inhibit PPIase activity.
It is striking that neither investigations on PPIase activity in human blood plasma or serum nor results on the pathophysiological significance of these enzymic activities in blood plasma or serum have been published.
For example, the total run time for monitoring the PPIase activity of just one sample takes about 20 min.
In this report, we describe the evaluation of this assay concerning both reliability and accuracy using human sera as the source of PPIase activity.
PPIase activities in sera were determined within 12 h after venipuncture.
Sequence analysis of peptidyl-prolyl cis-trans isomerase C (ppiC) from positive clones similar to 100% homology: Query--PPIase C sequence obtained by sequencing, subject-retrieved PPIase C sequence of S.
It may be concluded that ppiases catalyze the peptidyl-prolyl cis-trans isomerization, the ratelimiting step of protein folding, which is essential for newly synthesized protein to get its correct functional form.