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Serum albumin, human

Chloroplast-derived Biopharmaceuticals 8.3.2.1 Human Serum Albumin [Pg.118]


Dekker A, Beugeling T, Wind H, Post A, Bant]es A, Fei]en J and van Aken W G 1991 Deposition of oellular fibroneotin and dessorption of human serum-albumin during adhesion and spreading of human endothelial-oells on polymers J. Mater. Sol. 2 227-33... [Pg.2640]

Concerning the distribution of a drug, models have been published for log BB blood/brain partition coefficient) for CNS-active drugs (CNS, central nervous system) crossing the blood-brain barrier (BBB) [38-45] and binding to human serum albumin (HSA) [46]. [Pg.608]

Sulfaphenazole (684) and sulfazamet (685) are both examples of relatively short acting sulfonamides (B-80MI40406) and their antibacterial activity has been tested against Escherichia coli, the former being more effective than the latter. Sulfaphenazole also displaces sulfonyl ureas from protein binding sites on human serum albumin and consequently increases the concentration of the free (active) drug and produces a more intense reaction that may result in hypoglycemia. [Pg.291]

Human serum albumin has been purified similarly with 25% EtOH and 0.2% decanol. The isoelectric points of bovine and human serum albumins are 5.1 and 4.9. [Pg.511]

Proteins. A chiral stationary phase with immobilized a -acid glycoprotein on silica beads was introduced by Hermansson in 1983 [18, 19]. Several other proteins such as chicken egg albumin (ovalbumin), human serum albumin, and cellohy-drolase were also used later for the preparation of commercial CSPs. Their selectivity is believed to occur as a result of excess of dispersive forces acting on the more retained enantiomer [17]. These separation media often exhibit only modest loading capacity. [Pg.58]

Albumin (Human) Anti- Human-Serum-Albumin (Immuno-Reaction) not reacted antibody 0.1 M NaOH Ag2S 0.5-30 pg/ml... [Pg.255]

The resolution of these columns for protein mixtures, however, was comparably poor. The peak capacity for human serum albumin was near 3 during 20 min gradient elution. Improvement has been reached by covalent binding of PEI (M = 400-600) onto a 330 A silica of 5 pm particle size [38], The peak capacities of ovalbumin and 2a -arid glycoprotein were 30-40 (tgradienl = 20 min). Enhanced peak capacity and resolution probably were due to the more diffuse structure of PEI coupled to silane moieties than that of strictly adsorbed on silica and cross-linked (see Sect, 2.2). Other applications of covalently adsorbed PEI are discussed in Sect. 4.1. [Pg.147]

Antigens (e.g., bovine or human serum albumin, bovine gamma globulin, ovalbumin, penicillin)... [Pg.501]

Tissue plasminogen activators Human growth hormone Neuroactive peptides Regulatory peptides Lymphokines Human serum albumin Gamma globulin Antihemophilic factors Monoclonal antibodies... [Pg.35]

Monkos, Karol 2004. On the hydrodynamics and temperature dependence of the solution conformation of human serum albumin from viscometry approach. Biochimica et Biophysica Acta 1700, 27-34. [Pg.114]

Osborn BL, Olsen HS, NardeUi B, Murray JH, Zhou JX, Garcia A, Moody G, Zaritskaya LS, Sung C (2002) Pharmacokinetic and pharmacodynamic studies of a human serum albumin-interferon-alpha fusion protein in cynomolgus monkeys. J Pharmacol Exp Ther 303 540-548 Ozes ON, Reiter Z, Klein S, Blatt LM, Taylor MW (1992) A comparison of interferon-Conl with natural recombinant interferons-alpha antiviral, antiproliferative, and natural kiUer-inducing activities. J Interferon Res 12 55-59... [Pg.238]

Solubilization of biomolecules could induce change in the microemulsion structure. For example, in the presence of the human serum albumin and at low R value, the ternary microemulsion AOT/water/isoctane shows a transition to a bicontinuous microstructure [172],... [Pg.488]

Plasmepsin II. The malarial aspartyl protease plasmepsin II has a significant homology (35%) to cathepsin D. Correspondingly, the very same approach as for the cathepsin D inhibitors (see above) was followed. The best inhibitors have Ki values of 2-10nM, a molecular weight <650, moderate selectivity vs. cathepsin D, the most closely related human protease, log P values <4.6, and no apparent binding to human serum albumin, for example, compound 36 Ki plasmepsin II = 2.0nM, Ki cathepsin D = 9.8nM Fig. 16.5) [111]. [Pg.396]

Colmenarejo G, Alvarez-Pedraglio A and Lavandera JL. Cheminformatic models to predict binding affinities to human serum albumin. J Med Chem 2001 44 4370-8. [Pg.509]

Human serum albumin 582 amino acids 17 disulphide bridges Yeast Plasma replacement therapy Normally obtained from plasma but now concern over potential contamination with AIDS virus... [Pg.464]

Catalase has also been used as an enzyme label in competitive heterogeneous enzyme immunoassays. Catalase generates oxygen from hydrogen peroxide with the oxygen determined amperometrically with an oxygen electrode. This approach has been demonstrated for a-fetoprotein theophylline and human serum albumin... [Pg.33]

Hollosy, F., Valko, K., Hersey, A., Nunhuck, S., Keri, G., Bevan, C. Estimation of volume of distribution in humans from high throughput HPLC-based measurements of human serum albumin binding and immobilized artificial membrane partitioning. J. Med. Chem. 2006, 49, 6958-6971. [Pg.434]

HRA Histamine-releasing activity HRAN Neutrophil-derived histamine-releasing activity HRf Homologous-restriction factor HRF Histamine-releasing factor HRP Horseradish peroxidase HSA Human serum albumin HSP Heat-shock protein HS-PG Heparan sulphate protet ycan... [Pg.283]

There is a wide variety of commercially available chiral stationary phases and mobile phase additives.32 34 Preparative scale separations have been performed on the gram scale.32 Many stationary phases are based on chiral polymers such as cellulose or methacrylate, proteins such as human serum albumin or acid glycoprotein, Pirkle-type phases (often based on amino acids), or cyclodextrins. A typical application of a Pirkle phase column was the use of a N-(3,5-dinitrobenzyl)-a-amino phosphonate to synthesize several functionalized chiral stationary phases to separate enantiomers of... [Pg.12]

Takahashi, N., Takahashi, Y., Ishioka, N., Blumberg, B., and Putnam, F. W., Application of an automated tandem high-performance liquid chromatographic system to peptide mapping of genetic variants of human serum albumin, J. Chromatogr., 359, 181, 1986. [Pg.279]

Hanai, T., Miyazaki, R., and Kinoshita, T., Quantitative analysis of human serum albumin-drug interactions using reversed phase and ion-exchange liquid chromatography, Anal. Chim. Acta, 378, 77, 1999. [Pg.313]

Human serum albumin (HSA) may be used as a protectant against adsorptive loss of proteins present at low concentrations. HSA is present at higher concentration than the active substance and is preferentially adsorbed, coating the surface of interest and preventing adsorption of the drug. For example, insulin is subject to adsorptive loss to hydrophobic materials. Addition of 0.1-1.0% HSA has been reported to prevent this adsorptive loss [9],... [Pg.395]

Fig. 10 Release of cromolyn sodium (sodium cromoglycate) from human serum albumin microspheres prepared using a water-oil emulsion technique with 5% glutaraldehyde as cross-linking agent. Dissolution medium pH 7 phosphate buffer. (From Ref. 98.)... [Pg.554]


See other pages where Serum albumin, human is mentioned: [Pg.264]    [Pg.485]    [Pg.67]    [Pg.137]    [Pg.170]    [Pg.139]    [Pg.241]    [Pg.244]    [Pg.248]    [Pg.354]    [Pg.588]    [Pg.307]    [Pg.69]    [Pg.25]    [Pg.30]    [Pg.85]    [Pg.98]    [Pg.11]    [Pg.639]    [Pg.672]    [Pg.685]    [Pg.63]    [Pg.131]    [Pg.392]    [Pg.710]    [Pg.315]   
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Acidic drugs human serum albumin-drug

Albumin, human serum chemical derivatives

Albumin, human serum fractionated

Albumin, human serum fractionated electrophoresis

Albumin, human serum structure

Albumin, serum

Anti human serum albumin

Correlating 3D Structure to Human Serum Albumin Binding

Fragments from Human Serum Albumin

HAS, humane serum albumin

HSA, humane serum albumin

Human Serum Albumin with Laser Diode Excitation

Human Serum Albumin-Drug Binding Affinity Based on Liquid Chromatography

Human albumin

Human serum

Human serum albumin , drug transport

Human serum albumin Albumins

Human serum albumin Albumins

Human serum albumin acetate

Human serum albumin binding

Human serum albumin binding site

Human serum albumin capillary electrophoresis

Human serum albumin carrier

Human serum albumin chiral selectors

Human serum albumin chiral stationary

Human serum albumin chromatography

Human serum albumin data

Human serum albumin drugs that bind

Human serum albumin elution

Human serum albumin expression

Human serum albumin label

Human serum albumin lung profusion techniques

Human serum albumin oxidation

Human serum albumin separation from

Human serum albumin technetium-99 labelled

Human serum albumin tryptophan

Human serum albumin, HSA

Human serum albumin, antigenic

Human serum albumin, antigenic immunization

Human serum albumin, antigenic sites

Human serum albumin, assay

Human serum albumin, fluorescence immunoassay

Human serum albumin, preparation

Human serum albumin, stationary phase

Human serum albumin-drug

Human serum albumin-drug acidic compounds

Human serum albumin-drug analysis

Human serum albumin-drug binding affinity

Human serum albumin-drug binding constant

Human serum albumin-drug interactions

Human serum albumin-drug method

Human serum albumine

Human serum albumine

Human serum, albumin detection

Immunoassay human serum albumin

Iodine-125-human serum albumin

Normal human serum albumin

Protein human serum albumin

Size exclusion chromatography human serum albumin

Studies on Human Serum Albumin

Surface charge, human serum albumin

Warfarin/human serum albumin

Warfarin/human serum albumin binding

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