Proteins bromphenol blue

Protein (total) Fast green pH2 Ninhydrin—Alloxan Schiff s Mercuric-bromphenol blue... 

The dipstick test uses the bromphenol blue method for protein that is most sensitive for albumin and is optimized for protein levels/urine pH common in humans (Newman and Price 1999) False positives are thus common in animals because of their higher urine pH and background urine protein (Finco 1997 Loeb and Quimby 1999). A positive result with a urine dipstick test must therefore be followed by a more detailed quantitative and qualitative assessment of the increase in protein excretion in order to determine the site and nature of the renal injury present. 

Not only is the amount of dye bound to protein influenced by the nature and timing of the denaturation process (J5), but small changes in the ambient temperature may be important. An alcoholic dye bath produced 25% less bromphenol blue uptake by denatured albumin when the temperature was lowered from 20° to 0°C, but remained unaffected by a rise in temperature to 37°C (M15). 

Specimens of M reevesi were obtained from the collection of Norma Chapman, which is derived from feral populations in the U.K. Thirty adult males and females were examined. Preorbital sacs and Harderian glands were dissected out, fixed in 10% formalin, processed into paraffin and sectioned at 7 - 10 pm. Alternate slides of both the preorbital sac and the Harderian gland were stained with either haematoxylin and eosin or Mallory s stain. The remaining Harderian gland slides were treated with histochemical stains mucosubstances were detected by the periodic acid-Schiffs (PAS) method, whereas bromphenol blue (BPB) was used to detect protein (Barka and Anderson, 1965). For lipid detection, frozen Harderian gland sections (15Dm) were stained with the supersaturated isopropanol method (Oil Red O Lillie, 1961), using exposure to 70% alcohol as a control. 

Twenty fmol of 5 -radiolabeled single-stranded or double-stranded oligonucleotides is incubated with 1.3 pmol of the Rep protein (protein to DNA molar ratio of 60 1) for 5 min. The reaction is stopped by addition of 25 mM EDTA and 5 p.1 of loading buffer (30% glycerol, 0.25% xylene cyanol, and 0.25% bromphenol blue). The products are then loaded on a 8% polyacrylamide gel (30 1) in 5% glycerol, 0.25 x TBE, and run in 0.25 x TBE at room temperature. Incubation temperature is not important for migration under native conditions, and no differences are observed when protein and DNA are previously incubated together either at 105° and 4°. 

Figure 21. Isoelectric focusing in 5% polyacrylamide gdi 2% Ampholine carrier ampholytes, pH range 3.0-10.0. The left run represents laccase. The two runs to the right represent carhonic anhydrase B. Both samples were supposed to be very pure. Bromphenol blue staining according to Awdeh without fixation of proteins and without washing gel free from Ampholine. (Awdeh, Bruges conference 1969.)...

Terminate the run when the bromphenol blue tracking dye has reached the lower end of the gel and begin protein staining. 

Reaction termination. The reactions are terminated by the addition of SDS-PAGE sample buffer (10 mM Tris-HCl, pH 6.8, 1 mM EDTA, 1% DTT, 2.5-5% SDS, 0 01% bromphenol blue, final) followed immediately by boiling. Prepare a 4X stock of SDS-PAGE sample buffer and store in aliquots at -20°C. Quickly boiling the samples is essential to minimize artifactual proteolysis owing to bindmg-protein denaturation... 

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