Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Bromcresol Green”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources

Influence of plasma protein on the inhibitory effects of indocyanine green and bromcresol green on pulmonary prostaglandin E1 extraction.

The purpose of this study was to examine the influence of plasma protein on the inhibitory effects of the anionic dyes indocyanine green and bromcresol green on prostaglandin E1 (PGE1) uptake by the lungs. Dog lung lobes were isolated and perfused with either autologous plasma or Krebs-Ringer bicarbonate solution (KRB) containing no protein but with dextran used as a colloid. PGE1 uptake was determined by injecting a bolus, containing radiolabelled PGE1 into the lobar artery and then analysing ethanolic extracts of the venous effluent for radioactivity in PGE1 and PGE1 metabolites by thin layer chromatography and scintillation counting. When the lobes were perfused with KRB, bromcresol green at an average initial concentration of 28.5 microM, reduced PGE1 by an average of 56%. When the lobes were perfused with plasma, similar concentrations of bromcresol green reduced the uptake by less than 2%. A similar result was obtained with indocyanine green, which at an average initial concentration of 17.5 microM reduced uptake by about 70% when the lobes were perfused with KRB, but when the lobes were perfused with plasma similar concentrations of the dye reduced uptake by less than 3.5%. The results suggest that plasma protein binding interferes with the inhibitory effects of these dyes on PGE1 uptake in the lungs.

Alprostadil↗

Conversion between bromcresol green- and bromcresol purple-measured albumin in renal disease.

BACKGROUND: Albumin measured by a bromcresol purple dye-binding assay (Alb(BCP)) agrees more closely with the gold standard of immunonephelometry than does bromcresol green (Alb(BCG)) measurement. Both tests are in current clinical use. A method for converting between the two would be useful. METHODS: We measured albumin by bromcresol green and bromcresol purple in 535 patients, 155 of whom had renal disease. We randomly divided data from the patients with renal disease into two equal-sized sets, and used one set to derive, and the remaining set to validate, a regression equation relating the two values. RESULTS: The relationship Alb(BCG)=5.5+Alb(BCP) performed very well in both the renal patient validation set and in the data from 380 unselected in-patients and out-patients. Intraclass correlations for agreement between measured Alb(BCG) and predicted Alb(BCG) was 0.98 in both analyses. CONCLUSIONS: The ability to convert between these measurements will be of use in clinical situations where the absolute value of the serum albumin is important, when data from laboratories using different methodologies must be combined, and in the application of the Modification of Diet in Renal Disease formula to estimate glomerular filtration rate in patients whose albumin has been measured by bromcresol purple.

Bromcresol Green↗

Continuous-flow analysis for serum albumin, by use of the immediate reaction with bromcresol green.

Albumin reacts with bromcresol green reagent almost immediately, other serum proteins more slowly. This phenomenon can be exploited to improve the specificity of this routine method for determining serum albumin. I describe a 30-s reaction as adapted to continuous-flow analyzers, with no interference from other serum proteins. The method shows linearity to 72 g/liter. Results of this method correlate very well with those by the Laurell "rocket" and manual (30-s) bromcresol green methods. This procedure gives a considerable improvement in specificity for continuous-flow analyzers as compared with current bromcresol green methods.

Autoanalysis↗

An evaluation of the overestimation of serum albumin by bromcresol green.

Repeated observations have shown that the bromcresol green method overestimates serum albumin. Random patient serum samples were analyzed by a bromcresol green method using the Technicon AutoAnalyzer and by serum protein electrophoresis using cellulose acetate. The mean AutoAnalyzer value was 4.29 g/dl and the mean protein electrophoresis value was 3.68 g/dl (r = 0.915, slope = 0.869, y intercept = 1.090 g/dl where bromcresol green is on the Y axis, n = 166). Studies of the interference of proteins other than albumin in the bromcresol green method using the Technicon AutoAnalyzer showed that alpha globulins produce approximately a third, beta globulins a ninth, fibrinogen a fifth and hemoglobin equal the color intensity with the bromcresol green reagent that a comparable weight of albumin produced. In the bromcresol green method using the Du Pont ACA the interferences were even greater. At present, serum protein electrophresis is the most reliable method generally available to measure serum albumin. A modified bromcresol green method or immunoassay may eventually prove to be the method of choice.

Blood Protein Electrophoresis↗

Characterization of components of heat-treated serum albumin with bromcresol green.

The interactions of bromcresol green with various components isolated from heat treated bovine serum albumin at 65 degrees C and pH 9.0 were studied spectrophotometrically. The difference spectra of the dye induced by native albumin and component 1, which has the same electrophoretic mobility as native albumin, had a trough at 616 nm and peak at about 668 nm, whereas those induced by the denatured monomer (component 1'), denatured dimer (component 2) and denatured trimer (component 3) had a trough at 610 nm and peak at 655 nm. From these difference spectra, it was concluded that component 1 is a mixture of at least two components (native and modified native forms) and that components 1', 2 and 3, formed during the process of denaturation, have essentially the same conformation in the environment of the binding sites for bromcresol green. A possible mechanism for the heat denaturation of serum albumin is proposed.

Binding Sites↗

Time course of the effects of phenobarbital on biliary flow and on the biliary excretion of bromcresol green in rats.

Biliary flow and the biliary excretion of bromcresol green were measured in rats injected i.p. with a single dose of phenobarbital, 75 mg/kg. Biliary flow began to increase 6 h after the injection, it reached a peak at 36 h and returned to the control level at 72 h. In the same rats, the enhanced biliary excretion of bromcresol green was first observed at 12 h, it reached a peak at 24 h and returned to the control level at 72 h. Other groups of rats received 75 mg/kg phenobarbital as daily i.p. dose over 5 days. In these groups, the increase in biliary flow did not exceed that measured in the rats given the single dose, however, the biliary excretion of bromcresol green reached its peak after a 4-day phenobarbital treatment. After the 5th day of treatment the biliary flow and the biliary excretion of bromcresol green remained significantly stimulated for 4 days and the changes in these parameters regressed on the fifth day following the last injection of phenobarbital. The changes in liver weight appeared not to run closely parallel either with the increase in biliary flow or with the enhancement of biliary excretion of bromcresol green. It is suggested that the changes in biliary flow and in the biliary excretion of bromcresol green take place by different mechanisms after phenobarbital administration.

Animals↗

Improved specificity of serum albumin determination and estimation of "acute phase reactants" by use of the bromcresol green reaction.

The reaction of serum samples with bromcresol green proceeds in two steps. Albumin is responsible for the faster (less than 1 min) reaction; the slower (30-min) reaction is a measure of "acute phase reactant(s)" in serum. Serum is simply mixed with bromcresol green reagent and the absorbance is measured twice, immediately and at 60 min. Albumin concentrations, determined from the absorbance at 0 min, correlate well with those determined by Laurell "rocket" immunoelectrophoresis; r = 0.95 with no certain deviation from unity for the slope and with a negligible difference at zero concentration. The slow reaction was expressed as deltaA% = 100 (deltaAs/deltaAv) where deltaAs and delta Av are the changes in absorbance between 60 and 0 min for the sample and a commercial control serum, respectively. The value for deltaA% correlates well with the percentage of alpha2-fraction as determined by electrophoresis on cellulose acetate, as well as with orosomucoid and ceruloplasmin, all of which are acute phase reactant(s). Whether these proteins or other acute phase reactant(s) actually cause the slow reaction has not yet been established.

Bromcresol Green↗

Albumin standards and the measurement of serum albumin with bromcresol green. 1971.

A rapid and reliable method for measuring serum albumin employing bromcresol green is described. The addition of albumin to a solution of bromcresol green in a 0.075 M succinate buffer pH 4.20 results in an increase in absorbance at 628 nm. The absorbance-concentration relationship is linear for samples containing up to 6 g/dl albumin. Bilirubin, moderate lipemia, and salicylate do not interfere with the analysis. The use of nonionic surfactant (Brij-35) reduces the absorbance of the blank, prevents turbidity and provides linearity. The results by this method agree very well with those obtained by electrophoresis and salt fractionation. The method is simple, it has excellent precision and the reagents are stable. A protein standard is introduced which can be employed for both the total serum proteins and albumin determinations.

Blood Chemical Analysis↗

Spectrophotometric promethazine hydrochloride determination using bromcresol green.

A spectrophotometric method was developed for determining promethazine hydrochloride (I) complexed with bromcresol green and then extracted with chloroform. The complex in chloroform showed maximum absorption at 415 nm and obeyed Beer's law over 1.2-8.5 micrograms/ml. The complex molar absorptivity was 1.93 X 10(4) M. Complex formation and extraction were complete and quantitative over pH 2.7-2.8. The promethazine hydrochloride-bromcresol green molar ratio was 1:1. Excipients, coloring matter, flavoring agents, and other substances likely to be present in promethazine preparations did not interfere in the determination. Direct determination in tablet, syrup, and injection preparations were carried out satisfactorily.

Bromcresol Green↗

Bromcresol green assay is nonspecific for rat plasma albumin.

Bromcresol green (BCG) assay has been used in microvascular studies to determine albumin in rat plasma. The purpose of this study was to demonstrate that BCG overestimates rat plasma albumin partly because BCG binds to transferrin, a beta-globulin. The light absorbance of a transferrin-BCG reagent solution is shown to increase with time; appreciable binding occurs within a few seconds. Pure transferrin produced BCG assay results (P less than 0.001) that could be expressed as pseudoalbumin concentrations. Albumin and transferrin solutions of equal concentrations were mixed in equal parts; a plot of albumin concentration determined by BCG vs. actual albumin concentration had a slope greater than the expected value of 1.0 (P less than 0.001). Plasma samples were obtained from six rats and assayed for albumin. Electrophoresis yielded a plasma albumin of 2.97 +/- 0.11 g/dl, whereas BCG assay yielded a significantly (P less than 0.01) greater value of 3.58 +/- 0.07 g/dl. We conclude that BCG assay estimates of albumin-to-globulin ratio (A/G), in which G is determined from the difference between total protein and albumin, are especially subject to error.

Animals↗

The immediate reaction between bromcresol green and serum as a measure of albumin content.

I investigated the immediate ( less than 30s) reaction between bromcresol green and serum, as a measure of albumin content. Fifty sera were analyzed in duplicate for albumin by electrophoresis on cellulose acetate by a procedure previously shown to give results in good agreement with two immunoprecipitation techniques, and by a bromcresol green method with the absorbance being read as soon as possible after mixing. Results by the dye method were 3.0 g/liter higher than those by electrophoresis; this difference was independent of the albumin content of the serum. Slight turbidity, jaundice, or added hemoglobin did not significantly interfere with albumin determination. Aparently the immediate reaction between serum and the dye reagent provides a simple, reliable measure of albumin content when 3.0 g/liter is subtracted from the result obtained.

Bromcresol Green↗

[An improved method for selective determination of serum albumin by the bromcresol green method, using the SMAR 12/60 (author's transl)].

The estimation of serum albumin obtained with SMAR 12/60 by the bromcresol green method are in good agreement with values determined by electrophoresis only in the normal range. Interestingly marked discrepancies occur in the clinically relevant cases of hypalbuminosis. The shortening of the reaction time between bromcresol green and serum results in a better agreement between the values obtained with SMAR 12/60 and the values determined by electrophoresis over the whole range.

Autoanalysis↗

Comparison of manual methods of determination of albumin in human cerebrospinal fluid by the bromcresol green and immuno-precipitation methods.

Simultaneous determinations of albumin concentrations in human cerebrospinal fluid were made by three different manual methods: bromcresol green dye-binding technique of Doumas et al., a modification of the latter with color measurement shortly after the addition of dye as proposed by Ingwersen and Raabo and finally by an immuno-precipitation technique. Results obtained by the immuno-precipitation method correlated significantly with the dye-binding method of Doumas et al., (r = 0.93) and the procedure of Ingmersen and Raabo (r = 0.94). Data from the two dye-binding techniques correlated significantly with one another also (r = 0.98). However, the immuno-precipitation technique gives albumin values lower than the dye-binding procedures. The latter presumably estimates other proteins which can also bind bromcresol green. The data corroborates the conclusions of earlier investigators that immuno-precipitation method is more specific for albumin assays.

Adult↗

Albumin I.M.V.S.: a variant detected by a Bromcresol Green dye binding method.

A unique variant of human albumin was discovered in a family following routine multiple biochemical analysis. Their sera demonstrated increased Bromcresol Green (BCG) dye binding under certain reaction conditions (excess amounts of the detergent Pegosperse in the presence of Merthiolate). This effect was also seen with a structurally similar dye, Bromcresol Purple (BCP). The variant sera also showed an altered pattern of BCG dye binding (in the presence of Merthiolate and excess Pegosperse) compared to normal sera when the temperature or the pH of the dye reagent was changed. Decreased binding of the dye 2-(4'-hydroxybenzeneazo)benzoic acid (HABA) was also noted. Similar findings were observed in six other patients over a period of 21 months. Column chromatography of the variant sera on a DEAE-Sepharose column separated the albumin into two fractions, one showing normal dye binding properties, the other showing the more extreme pattern of dye binding seen for the whole variant serum.

Autoanalysis↗

Automated stopped-flow analyser in clinical chemistry: determination of albumin with bromcresol green and purple.

We describe an adaptation of a microcomputer-controlled stopped-flow analyzer for automated analysis of albumin in serum. The immediate reaction between bromcresol green or purple and albumin is used to develop a routine procedure with 12 s reaction time. The approach shows excellent linearity to 68 g/l, good sensitivity, a relative SD of less than 0.5%, mean recovery 99.1%, high sample throughput (180 prediluted samples/h) and no significant interferences. The 'reaction time' related overestimation of albumin that appears in prolonged procedures is eliminated, and results with this method correlate well with those obtained using the more specific immunonephelometric method.

Autoanalysis↗

Urinary albumin determination by the immediate bromcresol green method.

It has been demonstrated recently that the reaction of serum samples with bromcresol green (BCG) reagent proceeds in two steps. Albumin is responsible for the immediate reaction while other serum proteins produce the slow reaction. In this paper the immediate BCG reaction has been used for the determination of urinary albumin concentration in patients with proteinuria by a slightly modified method with a primary pH adjustment of the urine and the use of a urine blank. Comparison of the immediate BCG method (y) with Laurell "rocket" technique (x) gave the following equation: y = 17.2 + 1.006x (n = 98; r = 0.99) mg/l. The coefficient of variation (within-day), C.V. (%), ranged between 0.9 and 2.7% depending on the albumin concentration. It is thus possible to carry out rapid, accurate and precise albumin determinations in urine samples using this simple method.

Albuminuria↗