Bromocresol Green as a Reagent for Serum Albumin

1968 ◽  
Vol 5 (2) ◽  
pp. 51-53 ◽  
Author(s):  
J. R. Harding ◽  
J. W. Keyser
2018 ◽  
Vol 56 (3) ◽  
pp. 436-440 ◽  
Author(s):  
Sigurd Delanghe ◽  
Wim Van Biesen ◽  
Nadeige Van de Velde ◽  
Sunny Eloot ◽  
Anneleen Pletinck ◽  
...  

AbstractBackground:Colorimetric albumin assays based on binding to bromocresol purple (BCP) and bromocresol green (BCG) yield different results in chronic kidney disease. Altered dye binding of carbamylated albumin has been suggested as a cause. In the present study, a detailed analysis was carried out in which uremic toxins, acute phase proteins and Kt/V, a parameter describing hemodialysis efficiency, were compared with colorimetrically assayed (BCP and BCG) serum albumin.Methods:Albumin was assayed using immunonephelometry on a BN II nephelometer and colorimetrically based on, respectively, BCP and BCG on a Modular P analyzer. Uremic toxins were assessed using high-performance liquid chromatography. Acute phase proteins (C-reactive protein and α1-acid glycoprotein) and plasma protein α2-macroglobulin were assayed nephelometrically. In parallel, Kt/V was calculated.Results:Sixty-two serum specimens originating from hemodialysis patients were analyzed. Among the uremic toxins investigated, total para-cresyl sulfate (PCS) showed a significant positive correlation with the BCP/BCG ratio. The serum α1-acid glycoprotein concentration correlated negatively with the BCP/BCG ratio. The BCP/BCG ratio showed also a negative correlation with Kt/V.Conclusions:In renal insufficiency, the BCP/BCG ratio of serum albumin is affected by multiple factors: next to carbamylation, uremic toxins (total PCS) and α1-acid glycoprotein also play a role.


2013 ◽  
Vol 03 (03) ◽  
pp. 261-267 ◽  
Author(s):  
B. A. Olaniyan ◽  
X. Zhao ◽  
A. F. Mustafa

1980 ◽  
Vol 191 (1) ◽  
pp. 281-283 ◽  
Author(s):  
R G Reed ◽  
T Peters ◽  
S O Brennan ◽  
R W Carrell

Proalbumin Christchurch, a circulating variant of human serum albumin, is secreted from the liver without cleavage of the hexapeptide situated at the N-terminal end of the peptide chain of proalbumin. We compared ligand-binding properties of proalbumin Christchurch and of normal albumin A from the same individual in order to test the effect of the presence of the hexapeptide. The two albumin forms exhibited similar affinities for palmitate, bilirubin, 8-anilinonaphthalene-1-sulphonate and Bromocresol Green. The patterns of endogenous fatty acids bound to the two forms of albumin were slightly different, although the differences were probably not of physiological significance. From these studies it would appear that the propeptide of proalbumin does not alter the protein conformation in such a way as to alter binding sites for organic anions.


Author(s):  
D J Wright ◽  
L Biddulph ◽  
M G Rinsler

Serum free tri-iodothyronine (FT3), using two different radioimmunoassays, and serum albumin, using bromocresol green dye-binding method, were measured prospectively in 1374 adults investigated for thyroid disease. The results of similar pairs of measurements in 6608 serum specimens obtained from adults, but using one of the radioimmunoassays for FT3, were examined retrospectively. A close correlation was observed between the FT3 values and serum albumin concentration. Normalisation of the FT3 level using a standard albumin value of 43 g/L in the absence of chemical evidence of hypothyroidism (serum thyrotrophin <6·5 mIU/L) gave a distribution of FT3 values which closely resembled that from a normal population. The effects of acute illness and old age, which may lower the FT3 value, can be corrected by this transformation.


1974 ◽  
Vol 53 (1) ◽  
pp. 101-108 ◽  
Author(s):  
D. Webster ◽  
A.H.C. Bignell ◽  
E.C. Attwood

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