English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Protein disulfide isomerase (PDI) is known to contain the thioredoxin box motif with a low pKa cysteine residue. To investigate the reactivity of PDI with thiol modifiers at low physiological pHs, either the reduced (PDI[red]) or oxidized form (PDI[oxid]) of PDI was exposed to various alkylating ragents. When PDI was incubated with iodoacetamide at pH 6.3 for 30 min at 38C, a remarkable inactivation (&gt;90%) of PDI[red] was caused by iodoacetamide (IC[50]=8 M). However, PDI[oxid] was only slightly inactivated (approximately 18%) by iodoacetamide. Similarly, PDI[red] was significantly inactivated by Nethylmaleimide (NEM), but PDI[oxid] was not. When the inactivation by these alkylators was analyzed by pseudofirst order kinetics, NEM (k[3]=1.7510[-2] s[-1]; K[i]=124 M) was observed to be more potent than iodoacetamide (k[3]=9.110[-3] s[-1]; K=311 M). Interestingly, the inactivation of PDI[red] by iodoacetamide was greater at pH 6.3 than pH 7.0, in contrast to a similar inactivation potency of NEM at both pHs. Moreover, the maximal inactivation of PDI[red] or PDI[oxid] by iodoacetamide was mainly observed around pH 6.0. In addition, PDI[red] was found to be inactivated by acrolein (IC[50]=10 M) at pH 6.3, and this inactivation was also greater at pH 6.3 than at pH 7. Based on these results, we suggest that PDI[red] is susceptible to inactivation by alkylators including endogenous α,β-unsaturated aldehydes at low physiological pHs.

Inactivation of protein disulfide isomerase by alkylators including α,β-unsaturated aldehydes at low physiological pHs