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Cooperative Protein Folding by Two Protein Thiol Disulfide Oxidoreductases and 1 in Soybean.

Plant Physiol.. 2016; 
MatsusakiMotonori,OkudaAya,MasudaTaro,KoishiharaKatsunori,MitaRyuta,IwasakiKensuke,HaraKumiko,NaruoYurika,HiroseAkiho,TsuchiYuichiro,UradeR
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Recombinant Antibody Services Dot Far-western Blot Analysis Purified recombinant ER oxidoreductases and their variants as prey proteins were spotted onto a nitrocellulose membrane (GenScript) in a volume of 4 μL. Get A Quote

摘要

Most proteins produced in the endoplasmic reticulum (ER) of eukaryotic cells fold via disulfide formation (oxidative folding). Oxidative folding is catalyzed by protein disulfide isomerase (PDI) and PDI-related ER protein thiol disulfide oxidoreductases (ER oxidoreductases). In yeast and mammals, ER oxidoreductin-1s (Ero1s) supply oxidizing equivalent to the active centers of PDI. In this study, we expressed recombinant soybean Ero1 (GmERO1a) and found that GmERO1a oxidized multiple soybean ER oxidoreductases, in contrast to mammalian Ero1s having a high specificity for PDI. One of these ER oxidoreductases, GmPDIM, associated in vivo and in vitro with GmPDIL-2, was unable to be oxidized by GmERO1a. ... More

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