Disease relevance of Wool Blue RL

• In chromatin extracts of Novikoff hepatoma cells, six major periodic acid-Schiff-positive bands coincident with Coomassie Blue-stained protein bands were found with molecular weights of 30,000, 54,000, 64,000, 75,000, 104,000, and 127,000 [1].
• METHODS: CD146 was isolated from MEL-OH melanoma cells and characterized by Coomassie blue staining and Western blotting [2].
• In purified preparations of human erythrocyte GTP-binding proteins, we have identified a new substrate for pertussis toxin, which has an apparent molecular mass of 43 kDa by silver and Coomassie Blue staining [3].
• Silver staining of sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels revealed distinctive patterns for each serogroup and other Legionella species that were not observed by staining with Coomassie blue and may result from the presence of lipopolysaccharide in the membrane preparations [4].
• The expression of the protein is not toxic for E. coli cells and can be readily visualized by Coomassie blue staining of total bacterial protein extracts separated in polyacrylamide gels [5].

High impact information on Wool Blue RL

• Detergent lysates of unlabeled U937 cells, purified by affinity chromatography on anti-Id-Sepharose, yielded the same two nonreduced proteins and five reduction products in slab gels stained with Coomassie blue [6].
• Sodium dodecyl sulfate-analysis of the purified Ro/SSA antigen and analysis by staining of bands with silver and Coomassie Blue, Western blotting, and RNAase treatment leads to a hypothesis for the structure of the particle in which an antigenic 60,000 protein is bound to 24,000-27,000 RNA molecules which are not antigenic [7].
• Proteins were quantitated according to relative mass, as measured by the incorporation of a mixture of 15 3H-amino acids into secretory proteins contained in tissue slices, and according to the distribution of Coomassie blue R stain among proteins contained in pancreatic juice, as determined by two-dimensional gel scanning and computer analysis [8].
• Densitometry of Coomassie blue-stained polyacrylamide gels revealed that for each inner dynein arm subform, binding to axonemes was saturable and stoichiometric [9].
• We resolved four major Coomassie Blue-stained proteins with apparent molecular masses of 197, 200, 205, and 210 kD on high resolution one-dimensional SDS-polyacrylamide gels of mouse optic axons (optic nerve and optic tract) [10].

Chemical compound and disease context of Wool Blue RL

• Nitrilotriacetate (NTA), as the monohydrated trisodium salt, was administered by gavage to male Sprague-Dawley rats at levels of 0, 0.73 or 7.3 mmol/kg body weight/day for periods of up to 30 days [11].

Biological context of Wool Blue RL

• Coomassie blue-stained, heat-dried, and computer-imaged two-dimensional gels used to develop comprehensive human protein data bases served as the protein source to generate partial amino acid sequences [12].
• With longer phosphorylation, the 47-kD band showed increasingly lower mobility demonstrable both by Coomassie blue staining and autoradiography, suggesting both that it was multiply phosphorylated, and that the excisable band was pure [13].
• The ability of each protein kinase inhibitor to inhibit proliferation was also studied using four independent indices of ASM cell growth and division: 3-(4,5-dimethylthiazol-2-yl)2,5-diphenyl tetrazolium bromide (MTT) dye conversion, Coomassie blue protein determination, hemacytometer cell counts, and DNA synthesis [14].
• Hydrolysis of 2 is negligible below pH 9 and its hydrogenation results in formation of [Rh(CO)H(tppms)3] (5), which is an analogue to the well known and industrially used hydroformylation catalyst [Rh(CO)H(tppts)3] (6) (TPPTS = 3,3',3''-phosphinetriyltris(benzenesulfonic acid) trisodium salt) [15].
• Analysis of nuclear proteins and their states of phosphorylation by two-dimensional gel electrophoresis and autoradiography showed only minor changes in the species of proteins detectable by Coomassie Blue staining during the vegetative growth and development phases [16].

Anatomical context of Wool Blue RL

• SDS PAGE of the coated vesicle preparation followed by Coomassie Blue staining of proteins reveals a protein composition also typical of coated vesicles [17].
• On the basis of relative synthesis among lymphocyte proteins and detection by Coomassie blue staining, we also conclude that eIF-4D is a major cell protein [18].
• Many of the proteins detected by the silver stain in urine, spinal fluid, amniotic fluid, and cells were undetected with the widely used Coomassie blue stain [19].
• Enzyme-linked immunoelectrotransfer blots of the patients' erythrocyte membranes using a monoclonal antibody to protein 4.1 revealed that, in addition to protein 4.1, two other bands below protein 4.2 were stained; one of these bands migrated in the same position as the additional band detected in the Coomassie Blue-stained gels [20].
• Arterial smooth muscle myosin contains nonphosphorylated and phosphorylated light chains that appear as 4 spots on two-dimensional, Coomassie blue-stained gel electrophoretograms at the 20,000-molecular weight level (referred to as spots 4 through 1 in order of decreasing isoelectric points) [21].

Associations of Wool Blue RL with other chemical compounds

• SDS PAGE gels of the 6 M urea extract showed one major band at 70,000-mol-wt by Coomassie Blue staining [22].
• The radiolabeled doublet comigrated with a Coomassie Blue stained polypeptide doublet in the drug-resistant cells and was immunoprecipitated with polyclonal antibody which is specific for the 150-180-kDa surface membrane glycoprotein in multidrug-resistant cell lines [23].
• Each toxin position was substituted individually for a cysteine, which was then linked to a maleimido moiety through three different spacers, varying in length from 10 to 22 A. We estimated the coupling efficiency between the 15 toxin derivatives and the reduced cystine alpha(192-193) by gel densitometry of Coomassie Blue-stained gels [24].
• Major methylated membrane polypeptides were identified based on the comigration of radioactivity with Coomassie blue- and periodic acid-Schiff-staining species in pH 2.4 dodecyl sulfate gel electrophoresis, as well as by the distribution of radiolabel and protein following selective proteolysis and membrane extraction procedures [25].
• Estrogen-induced changes in membrane proteins and glycoproteins were also studied by Coomassie blue staining, periodic acid-Schiff staining, and autoradiography of 125I-concanavalin A binding following SDS-PAGE [26].

Gene context of Wool Blue RL

• Furthermore, SNF11 was detected in purified SNF-SWI complex by staining with Coomassie blue dye; its presence previously went unrecognized because it does not stain with silver [27].
• Failure of rhHsp70-1 to induce TNFalpha release was not because of defective physical properties since rhHsp70-1 and rhHsp70-2 contained identical hsp70 content as determined by SDS gels stained with Coomassie Blue and Western blots probed with an anti-rhHsp70 antibody [28].
• Failure of rhHSP60-1 to induce TNF-alpha release was not due to defective physical properties because rhHSP60-1 and rhHSP60-2 contained a similar amount of HSP60 as determined by SDS gels stained with Coomassie Blue and Western blots probed with an anti-rhHSP60 antibody [29].
• Antisera raised against purified chicken GAPDH reacted with a 36K protein present in chick brain extracts and estimated to be the fourth most prevalent protein, as determined by either Coomassie Blue staining or by in vitro translation of chick brain mRNA [30].
• The proteins were visualized by Coomassie blue staining and immunoblotting with specific antibodies to glial fibrillary acidic protein (GFAP) and vimentin [31].

Analytical, diagnostic and therapeutic context of Wool Blue RL

• It contained approximately 1% of the total amount of protein found in the original CEP-Si, corresponding to a single band on analytical isoelectric focusing, stainable by Coomassie Blue and of isoelectric point of 4.25 [32].
• Platinum in various fractions was quantitated by atomic absorption spectrophotometry with electrothermal atomization; proteins were quantitated by te Bradford method with Coomassie blue dye [33].
• After autoradiography, the colonies on the filter paper are stained with Coomassie blue [34].
• Its mobility was similar to BF F but it appeared to have a lesser intensity after straining with Coomassie Blue, and it was demonstrated by crossed immunoelectrophoresis to be present in lower concentration [35].
• During the past two years, the performance of fluorescence-based protein detection methods has demonstrably eclipsed conventional technologies such as colloidal Coomassie Blue and silver staining with respect to detection sensitivity, quantitative accuracy and compatibility with modern protein identification and characterization procedures [36].

References