Disease relevance of PEG 8000

• An Escherichia coli clone encoding a single cohesin domain of the cellulosome-integrating protein CipA from Clostridium thermocellum was constructed, and the corresponding polypeptide was purified, treated with papain, and crystallized from a PEG 8000 solution [1].
• Carboxypeptidase 1 from the thermophilic eubacterium Thermus thermophilus (TthCP1, 58 kDa), a member of the M32 family of metallocarboxypeptidases, was crystallized by the sitting-drop vapour-diffusion method using PEG 8000 as the precipitant [2].
• In an attempt to examine the structural role of TRAP in the signal transduction pathway, TRAP from Staphylococcus aureus was overexpressed, purified and crystallized using PEG 8000 and 5% Jeffamine M600 (pH 7.0), as precipitants by hanging-drop vapour diffusion methods at 287 K [3].

High impact information on PEG 8000

• We have crystallized Trypanosoma brucei PGK in the presence of the bisubstrate analog, adenylyl 1,1,5,5-tetrafluoropentane-1, 5-bisphosphonate, and solved the structure of this complex in two different crystal forms at 1.6 and 2.0 A resolution, obtained from PEG 8000 and ammonium phosphate solutions, respectively [4].
• In addition to the pretreatment, 12.5% polyethyleneglycol with an average molecular weight of 8000 kDa (PEG 8000) was included in the transfection mixture containing the DNA complexes [5].
• Crystals were grown in 0.1 M HEPES pH 7.5, 10% PEG 8000 and 8% ethylene glycol complemented with 9 mM 1-s-octyl-beta-D-thioglucoside or 0.1 M glycine [6].
• The catalytic domain of death-associated protein kinase (DAPK) has been overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method with PEG 8000 and magnesium acetate as precipitants [7].
• Single well diffracting crystals are obtained after switching from the hanging-drop method to liquid-liquid diffusion in capillaries using PEG 8000 as precipitant [8].

Biological context of PEG 8000

• Here, the GK domain was subcloned, expressed as an intein fusion protein, purified without the intein and then crystallized at room temperature by the hanging-drop vapour-diffusion method using PEG 8000 as a precipitant [9].
• The supercoiling free energy of pUC19 DNA [2686 base pairs (bp)] was measured in various concentrations of PEG 8000 (polyethylene glycol; molecular weight 8000) by the topoisomer distribution method [10].
• In contrast, PEG 8000-phosphate systems partitioned IBs more efficiently as a discrete sediment within the lower phase, whilst the majority of micronised debris remained in the interphase [11].

Anatomical context of PEG 8000

• In the presence of or after exposure to PEG 3350 or PEG 8000, the protein could not be detected by Western blot analysis after SDS-PAGE suggesting that the protein failed to enter the gel even though other HeLa cell surface proteins were unaffected [12].

Associations of PEG 8000 with other chemical compounds

• A condition consisting of 18% PEG 8000, 0.1 M sodium cacodylate pH 6.5, 0.2 M calcium acetate yielded long needles that diffracted to 3.20 A [13].
• An ATP-binding domain of human Hsp70 protein has been crystallized in two major morphological forms at pH 7.0 in the presence of PEG 8000 and CaCl2 [14].
• Albumin showed very poor affinity for polyethylene glycol molecular weight (Mw) 1000 (30 M(-1)) and Mw 8000 (400 M(-1)) (PEG 1000 and PEG 8000) [15].
• Among polyethylene glycol (PEGs) of different molecular weights, PEG 8000 (0.5%, w/v) caused a slight increase in the enzyme titre, while Tween-20, Tween-40 and Tween-60 (0.03%, w/v) exerted a significant stimulatory effect on enzyme secretion [16].
• The HNF1beta-DNA complex has been prepared and crystallized by hanging-drop vapor diffusion in 6%(v/v) PEG 300, 5%(w/v) PEG 8000, 8%(v/v) glycerol and 0.1 M Tris pH 8 [17].

Gene context of PEG 8000

• Free protein S antigen is measured by the same technique but after precipitation of the protein S-C4b-bp complex by PEG 8000 [18].
• Crystals have been obtained using PEG 8000 as precipitant and cacodylate at pH 6.3 as buffer [19].
• Crystals of the extracellular fragment of FcalphaRI/CD89 have been grown at 291 K using PEG 8000 as precipitant [20].
• Trigonal crystals of native BSDL, with unit-cell parameters a = b = 90.0, c = 156.1 A, were obtained using 15-20%(w/v) PEG 8000 as precipitant [21].
• Here, human UGDH (hUGDH) was purified and crystallized from a solution of 0.2 M ammonium sulfate, 0.1 M Na cacodylate, pH 6.5, and 21% PEG 8000 [22].

Analytical, diagnostic and therapeutic context of PEG 8000

• Here, the crystallization of infestin 4 using the sitting-drop vapour-diffusion method with PEG 8000 as precipitant is described [23].
• However, concentration-independent quantitative recovery of vincristine in saline solutions could be obtained by passivating the ultrafiltration devices with PEG-8000 and device drug adsorption was ameliorated for both agents by plasma [24].
• We also investigated the effect of addition of PEG 8000 to PCR reaction mixtures on the compatibility of materials [25].

References