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At least 19 recordsLinked to original sources

Dichromatism of bromphenol blue, with an improvement in the mercuric bromphenol blue technic for protein.

Staining of protein in sections using the mercuric bromphenol blue technic is improved by staining with 1% HgCl2 and 0.05% bromphenol blue in 2% aqueous acetic acid for 15 min at room temperature. Rinse slides 20 min in 2 changes of 0.5% aqueous acetic acid. Blot and give 2 fast changes in absolute ethanol with agitation before transferring to xylene. Transfer slide to 0.5% n-butylamine in xylene for a few seconds until the section is blue, then, after 2 changes of xylene, mount in DPX. Spectrophotometric analysis of this blue dye at different concentrations and with or without heparin showed that the reddish hues are due to dichromatism and not metachromasia.

Animals↗

Enhancement of pulmonary drug absorption in the rat by bromphenol blue and related dyes.

1. Pulmonary absorption studies in the rat showed that intratracheally administered 5-10 mM bromphenol blue, bromcresol green and bromthymol blue markedly increased the absorption rate of 0.1 mM phenol red. 2. Similarly, 1-10 mM bromphenol blue increased the absorption rate of 0.1 mP p-,minohippuric acid, tetraethylammonium and mannitol by 2- to 18-fold in a concentration-dependnet manner. 3. Mannitol absorption was enhanced more by bromthymol blue, sulphobromophthalein, bromcresol purple, thymol blue and bromcresol green than by bromphenol blue or m-cresol purple. Chlorphenol red and phenol red had no effect on mannitol absorption. 4. The results indicated that certain sulphonic acid dyes increase the permeability of the respiratory tract epithelium, perhaps by increasing its porosity.

Aminohippuric Acids↗

[Determination of residual bilirubin binding capacity in the serum of newborn infants using bromphenol blue].

In serum specimens collected from premature infants the residual bilirubin binding capacity was determined by a direct spectrometric method using bromphenol blue. The bindingin capacity determined in this way is strongly correlated to the serum bilirubin level. Changes in binding capacity are shown during the first 16 days of life. Experiments on model sera show the dependence of binding capacity for bromphenol blue on the ratio albumin/bilirubin. The results are discussed with respect to the urgency of blood exchange transfusions preventing danger of kernicterus.

Bilirubin↗

Kinetic assay of human pepsin with albumin-bromphenol blue as substrate.

A novel substrate, albumin complexed with bromphenol blue, has been developed for the assay of human gastric juice pepsin by a kinetic method in the Cobas centrifugal analyzer. The action of pepsin on the complex degrades the albumin and releases the dye. The change in the color of the substrate is a zero-order reaction. Human and porcine pepsin have different Km's with the new substrate. This kinetic method has a throughput of 28 tests in approximately 10 min and good precision (CV = 2.0%). Other advantages are analysis in homogeneous solution (thereby eliminating the need to separate substrate and products), lack of interference from bilirubin or phenol red, and the expression of pepsin activity in IUB enzyme units.

Albumins↗

[Selective, time dependent accumulation of the triphenylmethane dyes bromphenol blue, bromoresol green and iodophenol blue in mouse tumors].

1. A selective late dye concentration dependent on the time is described for 3 triphenylmethane dyes namely bromphenol blue, bromcresol green and iodophenol blue after intravenous application in high dosage in malignant inoculated tumors and experimental tumor metastases in the mouse. 2. The possible mechanisms of this dye concentration phenomenon in the tumor tissue as well as some chances of the eventual therapeutic and tumor diagnostic utilization were discussed.

Animals↗

Available bilirubin binding sites of serum from newborns determined by a direct spectrometric method using bromphenol blue.

A new direct spectrometric micromethod for the determination of the available bilirubin binding sites of serum (S-ABBS) using bromphenol blue has been applied to 298 blood specimens collected from infants immediately before starting the first exchange transfusion. A relative number fraction of 0.07 of the material, characterized by having the lowest S-ABBS values, includes seven of the nine cases (i.e. a relative number fraction of 0.78) with autoptically verified kernicterus (KI). The two infants with KI but higher S-ABBS values differed in having severe neurological symptoms before the examination. The mean substance concentration of bilirubin in these nine sera was 288 mumol/l. The correlation of KI to the body mass at birth, to the substance concentration of serum albumin, and to the substance concentration of serum bilirubin is given, and the sources of error concerning the method are discussed. The present method is proposed for determining a type of quantity that is important, among other types of data, in deciding on the need for exchange transfusion in icteric (premature) newborns.

Bilirubin↗

Simple spectrophotometric determination of urinary albumin by dye-binding with use of bromphenol blue.

This procedure for routine quantification of albumin in urine is based on the dye-binding properties of albumin with bromphenol blue. The absorbance of 100 microL of urine mixed with 3 mL of color reagent is measured against blank reagent at 610 nm after 30 s. Results vary linearly with albumin concentration up to 6 g/L. The reaction is pH independent in the physiological range. It is not subject to substantial interference by uric acid, creatinine, calcium, sodium chloride, or bilirubin. The presence of globulins produces a small positive error. Within-run precision (CV) was 4.8, 1.5, and 0.9%, and day-to-day precision was 11.2, 2.0, and 1.9%, for samples containing albumin at about 0.1, 1.0, and 6.0 g/L, respectively. Results by a radial-immunodiffusion method (x) correlated well with those by the proposed method (y): r = 0.986; y = 0.98x + 0.096; n = 64. The method can also be used to detect globulins, such as Bence Jones protein, by measuring the ratio of the absorbance at 30 min to that at 30 s.

Adolescent↗

A microalbuminuria assay using bromphenol blue.

A simple microalbuminuria assay using bromphenol blue/glycine reagent is described. Urine samples were prepared using gel filtration on Sephadex G-50 minicolumns and absorbance was measured at 610 nm 20 s after mixing 10 parts of eluate and 1 part of reagent. The detection limit of this method was 3 mg/l; within-run and between-run precision was between 0.5 and 4.1% for borderline and raised albumin concentrations. The recovery of albumin added to samples was 98.7 +/- 2.5%. Results obtained by this method correlated closely with values obtained by radial immunodiffusion (r = 0.987). The test is cheap (reagent costs about 5 cents) and suitable for the non-specialist laboratory.

Albumins↗

Absorption of phenol red and bromphenol blue as model drugs from the peritoneal cavity around the liver surface in rats.

The importance of the injection site on the pharmacokinetics of phenol red and bromphenol blue as model drugs after intraperitoneal administration into rat was examined. Their absorption rate from the peritoneal cavity was faster after intraperitoneal administration to the liver surface than that after intraperitoneal administration to the distal small intestine, as shown by the increase in maximum concentration and decrease in mean residence time in plasma. A similar tendency was observed in the biliary excretion pattern. The enhanced absorption rate was supported by the significantly smaller amount of both drugs remaining in the peritoneal cavity at 15 min after liver surface administration than that after small intestine administration. The liver concentration of the model drugs at 15 min after liver surface administration was 1.5-2.0 times that after small intestine administration. Accordingly, liver surface administration was shown to be effective with good absorption and efficient drug delivery to the liver.

Absorption↗

Effect of albumin on the absorption of phenol red, bromphenol blue and bromosulphonphthalein as model drugs from the liver surface membrane in rats.

The effect of bovine serum albumin (BSA) on drug absorption from the liver surface in rats was examined by using three organic anions (phenol red, bromphenol blue and bromosulphonphthalein) as model drugs which have a high affinity for albumin. The binding ratio of the model drugs (3 mg/ml in phosphate buffer) to BSA varied widely at a BSA concentration of 0.1--10% (w/v). The model drugs (3 mg/ml x 0.1 ml) with or without BSA were applied to the rat liver surface in vivo employing a cylindrical glass cell (i.d. 9 mm, area 0.64 cm2). The absorption ratios of the model drugs from the rat liver surface at 6h, calculated from the amount recovered from the glass cell, decreased with an increase in BSA concentration. A similar trend was observed with biliary recovery of the model drugs. A marked reduction in the absorption ratio was seen with bromosulphonphthalein, which has the highest binding activity to BSA among the three organic anions. Accordingly, protein binding appears to be a significant factor with respect to the drug absorption from the liver surface.

Absorption↗

Bromphenol blue: nitrate reductase activity in Nicotiana plumbaginifolia: an immunochemical and genetic approach.

NADH: nitrate reductase (EC 1.6.6.1) was purified from Nicotiana plumbaginifolia leaves. As recently observed with nitrate reductase from other sources, this enzyme is able to reduce nitrate using reduced bromphenol blue (rBPB) as the electron donor. In contrast to the physiological NADH-dependent activity, the rBPB-dependent activity is stable in vitro. The latter activity is non-competitively inhibited by NADH. The monoclonal antibody ZM.96(9)25, which inhibits the NADH: nitrate reductase total activity as well as the NADH: cytochrome c reductase and reduced methyl viologen (rMV): nitrate reductase partial activities, has no inhibitory effect on the rBPB: nitrate reductase activity. Conversely, the monoclonal antibody NP.17-7(6) inhibits nitrate reduction with all three electron donors: NADH, MV or BPB. Among various nitrate reductase-deficient mutants, an apoprotein gene mutant (nia. E56) shows reduced terminal activities but a highly increased rBPB:nitrate reductase activity. rBPB:nitrate reductase thus appears to be a new terminal activity of higher plant nitrate reductase and involves specific sites which are not shared by the other activities.

Antibodies, Monoclonal↗

A direct spectrometric method for determination of the concentration of available bilirubin binding sites in serum using bromphenol blue.

A simple and rapid direct spectrometric micromethod for the determination of the concentration of available bilirubin binding sites of serum is given. The method measures - by means of difference spectrometry - the maximal change in absorbance when serum is added to a buffered solution of bromphenol blue (BPB). This dye fulfills a set of requirements given and examined. The binding properties of bilirubin, BPB, and some related dyes are spectrometrically investigated, and differences between the properties of human and bovine albumin and between such albumin preparations and human serum are shown and discussed.

Adult↗

Use of bromphenol blue printing method for detecting sweat on the palm.

Sympathetic nerve fibres innervating the sweat glands in the skin are known to accompany sensory nerve fibres closely. Examination of sudorific function, therefore, is a useful aid in making a diagnosis of severed peripheral nerve and also provides valuable information on nerve function in the recovery stage following injury and surgery such as neurorrhaphy. Among the many methods which have been used clinically, the one employing bromphenol blue is thought to be the most simple and accurate.

Bromphenol Blue↗