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1998
DOI: 10.1039/a803429j
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Synthesis and interaction with human serum albumin of the first 3,18-disubstituted derivative of bilirubin

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Cited by 88 publications
(41 citation statements)
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“…The protein concentration was determined spectrophotometrically using the extinction coefficient of 35,219 M −1 cm −1 at 280 nm [19]. PEG-3000, PEG-6000 and mPEG-anthracene (0.25 mM) were dissolved in Tris-HCl solution (pH 7.4) and diluted to different concentrations.…”
Section: Preparation Of Stock Solutionsmentioning
confidence: 99%
“…The protein concentration was determined spectrophotometrically using the extinction coefficient of 35,219 M −1 cm −1 at 280 nm [19]. PEG-3000, PEG-6000 and mPEG-anthracene (0.25 mM) were dissolved in Tris-HCl solution (pH 7.4) and diluted to different concentrations.…”
Section: Preparation Of Stock Solutionsmentioning
confidence: 99%
“…The protein concentration was determined spectrophotometrically using the extinction coefficient of 36,500 M À1 cm À1 at 280 nm (Painter, Harding, & Beeby, 1998). A folic acid solution of 1 mM was prepared in 10 mM Tris-HCl and diluted to various concentrations in Tris-HCl (pH 7.4).…”
Section: Preparation Of Stock Solutionsmentioning
confidence: 99%
“…Human serum albumin (Structure 1) is a principal extracellular protein with a high concentration in blood plasma (40 mg ml -1 ) [15][16][17][18]. HSA is a globular protein composed of three structurally similar domains (I, II, and III), each containing two subdomains (A and B) and stabilized by 17 disulphide bridges [19][20][21][22]. Aromatic and heterocyclic ligands were found to bind within two hydrophobic pockets in subdomains IIA and IIIA, namely site I and site II [19][20][21][22].…”
Section: Introductionmentioning
confidence: 99%
“…HSA is a globular protein composed of three structurally similar domains (I, II, and III), each containing two subdomains (A and B) and stabilized by 17 disulphide bridges [19][20][21][22]. Aromatic and heterocyclic ligands were found to bind within two hydrophobic pockets in subdomains IIA and IIIA, namely site I and site II [19][20][21][22]. Seven binding sites are localized for fatty acids in subdomains IB, IIIA, IIIB, and on the subdomain interfaces [16].…”
Section: Introductionmentioning
confidence: 99%
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