نتایج جستجو برای: protein disulfide isomerase
تعداد نتایج: 1249610 فیلتر نتایج به سال:
The essential flavoenzyme Ero1p both creates de novo disulfide bonds and transfers these disulfides to the folding catalyst protein disulfide isomerase (PDI). The recently solved crystal structure of Ero1p, in combination with previous biochemical, genetic and structural data, provides insight into the mechanism by which Ero1p accomplishes these tasks. A comparison of Ero1p with the smaller fla...
Native disulfide bond formation in eukaryotes is dependent on protein-disulfide isomerase (PDI) and its homologs, which contain varying combinations of catalytically active and inactive thioredoxin domains. However, the specific contribution of PDI to the formation of new disulfides versus reduction/rearrangement of non-native disulfides is poorly understood. We analyzed the role of individual ...
Eukaryotic protein disulfide isomerase (PDI) is a 55-kDa enzyme with cysteine oxidoreductase, chaperone, and antichaperone activities that catalyzes disulfide formation and rearrangement in the eukaryotic endoplasmic reticulum. In Gram-negative bacteria, the formation of disulfide bonds in the periplasm is mediated by DsbA, a strong cysteine oxidase but an inefficient catalyst of disulfide bond...
مقدمه: scfv یکی از معروفترین قطعات حاصل از آنتی بادیهای تک دودمانی است و مخمر pichia pastoris یکی از مهمترین میزبان های بیانی اینگونه قطعات محسوب می شود. روش های بسیاری برای افزایش میزان بیان پروتئین های هترولوگ در این میزبان وجود دارد .باتوجه به اینکه فرایند تغییرات پس از ترجمه ای در شبکه آندوپلاسمی مرحله تعیین کننده سرعت در تولید پروتئین هاست، هدف قرار دادن چاپرون هایی نظیر pdi (protein disul...
The chemistry of disulfide exchange in biological systems is well studied. However, very little information is available concerning the actual origin of disulfide bonds. Here we show that DsbB, a protein required for disulfide bond formation in vivo, uses the oxidizing power of quinones to generate disulfides de novo. This is a novel catalytic activity, which to our knowledge has not yet been d...
The primary activity of protein disulfide isomerase (PDI), a multifunctional resident of the endoplasmic reticulum (ER), is the isomerization of disulfide bridges during protein folding. We isolated a cDNA encoding Dictyostelium discoideum PDI (Dd-PDI). Phylogenetic analyses and basic biochemical properties indicate that it belongs to a subfamily called P5, many members of which differ from the...
Background: Stomach ulcer is one of the diseases that many patients suffer from all over world, and it causes damage to intestinal wall. Some research has shown Bauhinia thonningii extract, which been traditionally used treat a variety ailments, including stomach ulcers, powerful antioxidant mucus-increasing properties. Objective:This aimed at studying mechanism(s) through methanolic (MBST) chl...
Trichlorophenol (TCP) is a widely used and persistent environmentally toxic compound that poses a carcinogenic risk to humans. Phytoremediation is a proficient cleanup technology for organic pollutants. In this study, we found that the disulfide isomerase-like protein AtPDIL1-2 in plants is a good candidate for enhancing 2,4,6-TCP phytoremediation. The expression of AtPDIL1-2 in Arabidopsis was...
8 3.1. Catalysis of oxidative protein folding 8 3.2 De novo formation of disulfide bonds in E. coli: the discovery of DsbA 9 3.3. DsbA is the most oxidizing disulfide catalyst 11 3.4. DsbB provides the periplasm with oxidizing power 15 3.5. Correcting wrong disulfide bonds in the periplasm: disulfide bond isomerization by DsbC 18 3.6. DsbD provides reducing equivalents in a highly oxidizing env...
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