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Serum, human

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]

In this chapter we will discuss immunoglobulins of the IgG class, which is the major type of immunoglobulin in normal human serum, and which has the simplest structure. Each chain of an IgG molecule is divided into domains of about 110 amino acid residues. The light chains have two such domains, and the heavy chains have four. [Pg.301]

Ega, or PGEgQ, is present in human serum at a level of less than M.Hn addition, they often have half-lives of only 30 seconds to a few minutes, not lasting long enough to be easily identified. Moreover, most animal tissues upon dissection and homogenization rapidly synthesize and degrade a variety of these substances, so the amounts obtained in isolation procedures are extremely sensitive to the methods used and highly variable even when procedures are carefully controlled. [Pg.831]

Z. Liu, S. R. Siiimanne, D. G. Patterson-Jr, L. L. Needham and J. B. Phillips, Comprehensive two-dimensional gas cliromatography for the fast separation and determination of pesticides exrtacted from human serum . Anal. Chem. 66 3086-3092 (1994). [Pg.108]

M. Tanaka and H. Yamazaki, Dkect detemination of pantoprazole enantiomers in human serum by reversed-phase liigh peifomance liquid chi omatography using a cellulose-based cliiral stationaiy phase and column-switching system as a sample cleanup procedure , Aim/. Chem. 68 1513-1516(1996). [Pg.132]

Basic drugs human serum liq-liq extraction ion-pair C18 C18 UV 37... [Pg.255]

TCV-116and its metabolites human serum/urine liq-liq extraction CIS CIS Elu 64... [Pg.256]

Various drugs human serum/plasma none micel C8 orCN CIS UVorElu 33... [Pg.256]

K. Yamashita, M. Motohashi and T. Yashiki, Column-switching techniques for high-performance liquid cliromatography of ibuprofen and mefenamic acid in human serum with shoit-wavelength ultraviolet detection , J. Chromatogr. 570 329-338 (1991). [Pg.293]

T. Miyabayashi, K. Yamashita, E Aoki, M. Motohashi, T. Yashiki and K. Yatani, Determination of manidipine and pyridine metabolite in human serum by liigh-perfor -mance liquid cliromatography with ultraviolet detection and column switching , J. Chromatogr. 494 209 - 217 (1989). [Pg.293]

T. Hyotylainen, T. Andersson and M. E. Riekkola, Eiquid cliromatographic sample cleanup coupled on-line with gas chromatography in the analysis of beta-blockers in human serum and urine , 7. Chromatogr. Sci. 35 280-286 (1997). [Pg.299]

Today, however, GC-GC coupling is seldom used to determine pesticides in environmental samples (2), although comprehensive MDGC has been applied to determine pesticides in more complex samples, such as human serum (19). On the other-hand, new trends in the pesticide market, which is now moving towards the production of optically active enantiomers and away from racemic mixtures, may make this area suitable for GC-GC application. The coupling of non-chiral columns to chiral columns appears to be a suitable solution to the separation problems that such a trend might cause. [Pg.337]

Comprehensive two-dimensional GC has also been employed for the analysis of pesticides from serum, which, although not strictly a forensic analytical problem , provides an example of the promise of this technique to forensic applications, such as the analysis of drugs of abuse (40). Two-dimensional gas chromatograms of a 17-pesticide standard and an extract from human serum are shown in Figure 15.13. The total analysis time of about 5 min, high peak capacity and the separation of all... [Pg.426]

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]

An affinity sorbent based on WPA-PG carrying immobilized human IgG was applied to the isolation of the first component of the complement (Cl) from human serum and for its separation into subcomponents Clr, Cls and Clq by the one-step procedure [126,127]. Cl was quantitatively bound to the sorbent at 0 °C. The activities of subcomponents Clq and Clr2r2 in the unbound part of the serum were found to be 0.8% and 3.3% of the initial activities in serum. This fraction, therefore, could be used as a R1 reagent for determining the hemolytic activity of Cl. Apparently, the neighboring macromolecules of immobilized IgG resemble to some extent an immune complex, whereas Cl formation is facilitated due to the mobility of polymer chains with the attached IgG macromolecules (Cl is usually dissociated in serum by 30%). After activation of bound Cl by heating (30 °C, 40 min) the activated subcomponent Clr is eluted from the sorbent. Stepwise elution with 0.05 mol/1 EDTA at pH 7.4 or with 0.05 mol/1 EDTA + 1 mol/1 NaCl at pH 8.5 results in a selective and quantitative elution of the activated subcomponent Cls and subcomponent Clq. [Pg.171]

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

FIGURE 4-18 Permselective coatings flow injection response of a poly(l,2-diaminoben-zene)-coated electrode to the following a, hydrogen peroxide (1 mM) b, ascorbic acid (1 mM) c, uric acid (1 mM) d, L-cysteine (1 mM) and e, control human serum. (Reproduced with permission from reference 63.)... [Pg.124]

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

Methyl parathion was determined in dog and human serum using a benzene extraction procedure followed by GC/FID detection (Braeckman et al. 1980, 1983 DePotter et al. 1978). An alkali flame FID (nitrogen-phosphorus) detector increased the specificity of FID for the organophosphorus pesticides. The detection limit was in the low ppb (pg/L). In a comparison of rat blood and brain tissue samples analyzed by both GC/FPD and GC/FID, Gabica et al. (1971) found that GC/FPD provided better specificity. The minimum detectable level for both techniques was 3.0 ppb, but GC/FPD was more selective. The EPA-recommended method for analysis of low levels (<0.1 ppm) of methyl parathion in tissue, blood, and urine is GC/FPD for phosphorus (EPA 1980d). Methyl parathion is not thermally stable above 120 °C (Keith and Walters 1985). [Pg.175]


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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

Analysis of Lycopene Stereoisomers in Tomato Extracts and Human Serum

Anti human serum albumin

Applications to human serums

Carotenoid in human serum

Cobalamins in Human Serum

Correlating 3D Structure to Human Serum Albumin Binding

Fragments from Human Serum Albumin

Glucose in human serum

Glycoproteins serum, human

HAS, humane serum albumin

HSA, humane serum albumin

Hemoglobin human serum fractionated

Human Serum Albumin with Laser Diode Excitation

Human Serum Albumin-Drug Binding Affinity Based on Liquid Chromatography

Human Serum Copper and Ceruloplasmin Levels with Age

Human blood serum

Human cerebrospinal fluid serum

Human cord serum

Human exposure blood serum

Human placental serum

Human sera, testing

Human serum SRM

Human serum albumin

Human serum albumin , drug transport

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 analysis

Human serum cholesterol

Human serum cholesterol, plant

Human serum chorionic gonadotrophin

Human serum creatinine determination

Human serum electrophoresis

Human serum fractionated

Human serum general considerations

Human serum glucose determination

Human serum lipoprotein analysis

Human serum lipoproteins

Human serum oxidative damage

Human serum paraoxonase

Human serum potential improvements

Human serum protein damage

Human serum proteins

Human serum transferrin

Human serum, PCDD

Human serum, albumin detection

Human serum, lactic dehydrogenase

Human serum, pooled

Humans serum lipid changes

Immunoassay human serum albumin

Incidents exposure, human serum

Iodine-125-human serum albumin

Ligand binding interactions, human serum

Microspheres, human serum

Normal human serum albumin

Peptide human serum

Protein human serum albumin

Protein human serum fractionated

Serum charged with human

Serum, human, exposure

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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