Circular dichroism and hydrodynamic measurements of ternary protein—Two ligand systems: Serum albumin-bilirubin-drug or alcohol

Lavie, E.; Blauer, G.

doi:10.1016/0003-9861(79)90023-7

Cited by 7 publications

(4 citation statements)

References 33 publications

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“…In this respect, Taylor et al (1975) demonstrated that the 'enzyme-like activity' of bovine serum albumin in catalysing the decomposition of the Meisenheimer complex is exquisitely sensitive to the conformational integrity of the protein. Conformational changes in albumin by binding of ligands are widely documented in the literature (Beaven et al, 1973;Lavie & Blauer, 1979). We suggest this possibility in this case owing to the slight differences detected between the c.d.…”

Section: Discussionsupporting

confidence: 53%

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Identification of a liver growth factor as an albumin-bilirubin complex

Díaz-Gil¹,

Gavilanes²,

Sánchez³

et al. 1987

Biochemical Journal

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We have reported the purification and characterization of a protein that behaves as a liver growth factor, showing activity either in vivo or in vitro [Díaz-Gil et al. (1986) Biochem. J. 235, 49-55]. In the present paper, we identify this liver growth factor (LGF) as an albumin-bilirubin complex. This conclusion is supported by the results of chemical and spectroscopic characterization of this protein as well as by experiments in vivo. Incubation of albumin isolated from normal rats with bilirubin/albumin molar ratios (r) resulted (when r = 1 or 2) in a complex with liver DNA synthesis promoter activity identical with that of LGF. The exact amount of bilirubin bound to albumin was assessed by fluorescence and c.d. spectra. This albumin-bilirubin complex showed the same dose-dependence profile as LGF either at low or high dose of protein injected per mouse. Both LGF and albumin-bilirubin complex produced similar increases in the mitotic index of mouse hepatocytes in vivo. A new mechanism for the onset of the hepatic regenerative process is proposed.

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Section: Discussionsupporting

confidence: 53%

“…signal arising from bound bilirubin. It is known that albumin possesses two kinds of binding sites for bilirubin, one of high affinity and one or two of low affinity (Berde et al, 1979;Lavie & Blauer, 1979). Although the percentage of bound bilirubin was estimated from the c.d.…”

Section: Protein-chemical Similarities Between Lgf and Serum Albuminmentioning

confidence: 99%

Identification of a liver growth factor as an albumin-bilirubin complex

Díaz-Gil¹,

Gavilanes²,

Sánchez³

et al. 1987

Biochemical Journal

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“…Friedman and Lewis [6] showed that biliru bin was displaced in human cord serum in vitro by sulphafurazole, cloxacillin and flucloxacillin, but not by ampicillin, since the protein binding of the latter is less than 25%, whereas the binding of cloxacillin, flucloxacillin and sulphafurazole is over 90%. Lavie and Blauer [5], however, have reported ampicillin-displaced bilirubin from human serum albumin. Numerous clinical results with cefazolin and cephalothin, which have a high protein-binding affinity, indicate that these two antibiotics cause little or no displacement of bilirubin [ 10].…”

Section: Discussionmentioning

confidence: 96%

“…Investigators in pediatrics have called attention to drug-induced displacement of bilirubin serum albumin binding in new borns [2], Administration of salicylate and sulfisoxazole may cause bilirubin enceph alopathy due to the redistribution of bilir ubin to the extravascular tissue from the plasma of newborns with hyperbilirubin emia [5,9].…”

Section: Introductionmentioning

confidence: 99%

Effect of Ceftizoxime, a New Cephalosporin Antibiotic, on Binding of Bilirubin to Human Serum Albumin

Sakamoto¹,

Murakawa²,

Hirose³

et al. 1983

Chemotherapy

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An investigation and comparison of the competitive effect of ceftizoxime, a new cephalosporin, and other β-lactam antibiotics on in vitro binding of bilirubin to human serum albumin showed that at a normal range of serum albumin (3.48 g/di) and bilirubin (0.94 mg/dl) in healthy infants, free bilirubin did not increase in the presence of any of the test antibiotics at concentrations up to 640 μg/ml. When the albumin concentration was decreased to one-fifth of the normal human range, only ceftizoxime caused no bilirubin displacement.

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Kinetics of transfer in aqueous solution of ferriprotoporphyrin IX from human serum albumin to sperm whale apomyoglobin

Blauer

Silfen

1982

Biopolymers

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SynopsisKinetic aspects of the transfer reaction of ferriprotoporphyrin IX (FP) from its complex with human serum albumin (HSA) to sperm whale apomyoglobin were investigated by spectrophotometry in aqueous solution. At molar ratios of 2 1 of both HSA and apomyoglobin to FP (1 X 10-5M), the initial rate of transfer at pH 7.4 (0.025M Tris buffer) and 25'C was virtually independent of the concentration of apomyoglobin up to a sixfold excess of the latter. The rate-limiting step in the transfer reaction is considered to be the dissociation of FP from the FP-HSA complex with an apparent rate constant of the order of s-l under the above conditions. The initial rate decreased with increasing concentrations of HSA, indicating competition between HSA and apomyoglobin for free FP in the recombination reactions. A steady-state concentration of the order of 10-9M is estimated for free FP under the conditions given. The initial rate of transfer decreased markedly with pH in the range of pH 5-9 and was also dependent on the type and concentration of the buffer used. Also, various electrolytes at different concentrations showed very different and specific effects on the initial rate of reaction. Similarly, various drugs and analogous substances such as penicillins and salicylate affected the rates of dissociation in different concentration ranges. From the temperature dependence of the initial rate at pH 7.4 in the range of 5-25"C, an overall energy of activation of about 8 kcal/mol and an entropy of activation of about -50 e.u. are evaluated, indicating a much higher order of molecular groups around FP or other steric constraints in the transition state. It appears that kinetic parameters of the hiopolymer-small molecule system are more sensitive to environmental changes than corresponding equilibrium data as measured by light absorption.

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Circular dichroism and hydrodynamic measurements of ternary protein—Two ligand systems: Serum albumin-bilirubin-drug or alcohol

Cited by 7 publications

References 33 publications

Identification of a liver growth factor as an albumin-bilirubin complex

Identification of a liver growth factor as an albumin-bilirubin complex

Effect of Ceftizoxime, a New Cephalosporin Antibiotic, on Binding of Bilirubin to Human Serum Albumin

Kinetics of transfer in aqueous solution of ferriprotoporphyrin IX from human serum albumin to sperm whale apomyoglobin

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