HSA human serum albumin

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]. 

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],... 

Derrick studied the interaction of L-tryptophan and ibuprofen with human serum albumin (HSA),74 which is an abundant transport blood protein capable of binding efficiently several species.75 They acquired 1H NMR spectra of L-Tryptophan-HSA system for different ligand protein molar ratios, that is 3 1, 5 1, 7 1 and 10 1. The aromatic resonances of L-Tryptophan are difficult to be observed due to the overlap with HSA signals, even at 10 1 molar ratio, so that the spectral subtraction was performed. D values of L-Tryptophan were calculated by integration of the subtracted spectra and were in good agreement with those predicted by computer simulations. In the case of ibuprofen, only for 140 1 molar ratio, the resonances of ibuprofen are clearly visible also in this case, the... 

The noncovalent approach is based on the use of complexes containing suitable moieties which are able to recognize specific proteins, primarily human serum albumin (HSA). When the targeting protein is confined in the blood, the adduct between the serum albumin and the functionalized complex may function as a blood pool agent. Due to the reversible nature of binding between the protein and the paramagnetic chelate, these adducts maintain excretory pathways typical of small complexes which, from the pharmacological point of view, favors them over covalently bound macromolecules. 

Fig. 3.6 Human serum albumin (HSA) was produced during the sprouting of transgenic rape-seeds. A light-inducible Rubisco promoter was used to control transgene expression. The highest yield was obtained with light induction after three days of continuous darkness. Sprouting was carried out in an airlift fermentor at room temperature. The sprouting medium was water.

Consequently, the research work of Hara s group continued focusing on the improvement of protein determination using CE combined with online CL detection. By replacing EY by the Rhodamine B isothiocyanate (RITC) dye in the binary complexes formed with the proteins BSA or human serum albumin (HSA) and using a different imidazole buffer solution of pH 6, the sensitivity was increased [72], However, best detection limits for these determinations were found employing the tetramethylrhodamine isothiocyanate isomer (TRITC) dye, left for 4 h with a standard solution of BSA in acetonitrile followed by introduction into the capillary. For BSA, a detection limit of 6 nM was reached [73],... 

Investigations of the effects of UV- and hypochlorite-induced oxidative modification of 20 amino acids and human serum albumin (HSA) on their antiradical properties showed unexpected results [36], Seven amino acids (cystine, histidine, methionine, phenylalanine, serine, tryptophan, and tyrosine) and HSA developed ACW following oxidation (see examples in Fig. 14). The fresh (produced in 1998) HSA from Serva had no antiradical capacity, but it acquired this quality during irradiation. The out-of-date HSA sample (Dessau, GDR, 1987, expiration date 7/1/1992) showed a remarkable ACW even in an unirradiated state. 

Despite the undoubted advantages of recombinant production, it remains the case that many protein-based products extracted directly from native source material remain on the market. In certain circumstances, direct extraction of native source material can prove equally/more attractive than recombinant production. This may be for an economic reason if, for example, the protein is produced in very large quantities by the native source and is easy to extract/purify, e.g. human serum albumin (HSA Chapter 12). Also, some blood factor preparations purified from donor blood actually contain several different blood factors and, hence, can be used to treat several haemophilia patient types. Recombinant blood factor preparations, on the other hand, contain but a single blood factor and, hence, can be used to treat only one haemophilia type (Chapter 12). 

The protein A (pA), antihuman serum albumin (a-HSA, M 150 kD), and human serum albumin (HSA, M 65 kD) were provided by Paradocs BV (Tiel, The Netherlands). The Herpes Simplex Virus type 1 (HSV-1) and anti-HSV-1 gG glycoprotein G monoclonal antibody (a-HSV-1 gG) were purchased from Virusys Corporation (Marriottsville, MD, USA). Bovine serum albumin (BSA, M 50 kD) was purchased from Sigma-Aldrich Chemie BV (Zwijndrecht, The Netherlands). Synthetic surface protein of Hepatitis-B virus generated in Hep-G2 cell-line (HEP G2, M 25 kD) was provided by BioMerieux BV (Boxtel, The Netherlands). Phosphate buffered saline (PBS) was used for all experiments. 

Human relations, safety and, 21 857-858 Human serum albumin (HSA), yeast-derived, 26 485-486 Humans... 

Among the series of dyes, in which the effect of binding to human serum albumin (HSA) was studied [41], the dye 8 (Fig. 10) exhibited J-aggregate absorption and fluorescence bands, while these bands were not observed for the free dye. This led to the conclusion about the J-aggregation of the dye 8 in the HSA binding site. 

Proteins have, to date, only rarely been purified by SMB. The first attempt was made by Huang et al. in 1986 [42]. They isolated trypsin from porcine pancreas extracts using an SMB made of only six columns. In addition, this example also demonstrates that SMB systems with a very limited number of columns can be efficient. Another example for a successful protein-separation by SMB is the purification of human serum albumin (HSA) using two SMB-systems connected in series [43]. The first SMB was used for removing the less strongly retained components and the second one for removing the more strongly retained components of the sample matrix. 

Semm albumin is not an enzyme but a transport protein, yet it has demonstrated hydrolytic activity against a variety of xenobiotic substrates. This este-rase-like activity has been known for years, but there is still confusion in the literature regarding its nature and mechanism. Indeed, it was not clear whether this activity is intrinsic to the albumin molecule or results from contamination of albumin preparations by one or more hydrolytic enzymes. More-recent studies with highly purified human serum albumin (HSA) have confirmed that the protein has an intrinsic esterase activity toward several substrates, but that activity due to contaminants and particularly semm cholinesterase is involved... 

Fig. 3.17. The crystal structure of human serum albumin (HSA) complexed with four molecules ofmyristic acid (from lbj5.pdb [121][122]). The picture shows the domains (I—III) and subdomains (A and B) of HSA. The primary hydrolytic site is located in subdomain IIIA, and two others probably in subdomain IIA. 

Braun and Alsenz6 used an ELISA to detect aggregates in interferon-alpha (IFN-a) formulations. They analyzed IFN-a formulations for possible aggregate formation because all marketed interferons are reported to induce antibodies to some extent. Because of its stabilizing effects, human serum albumin (HSA) is used in the formulation of marketed IFN-a at a great excess over IFN-a itself. HSA can also interact with other proteins. Braun and Alsenz developed an ELISA for the detection of both IFN-a-IFN-a and HSA-IFN-a aggregates. A MAb was used for the capture and detection of the IFN-a and a polyclonal for the detection of HSA. The assay is shown schematically in Figure 11.4. 

The data presented here constitute part of the results attained in the development of a research project funded by the European Community (EC) and performed in cooperation with three independent European companies [6]. Hybrid polymeric materials based on intimate blends of human serum albumin (HSA), alkyl hemiesters of alternating copolymers of maleic anhydride (MAn), and vinyl ethers of monomethoxyoligoethylene glycols (PEGVE) were selected as biocompatible matrices for the formulation of the nanoparticles. 

The preparation and characterization of alternating copolymers of Maleic anhydride (MAn) and poly (ethylene glycol-vinyl ether) as well as their chemical conversions to provide various alkyl hemiesters (Scheme 1) have been described elsewhere [7]. The matrices are quoted as PAMm z, where m represent the number of oxyethylene units in R and n the number of carbon atoms in R. Human serum albumin (HSA) was provided by Isti-tuto Sierovaccinogeno Italiano SpA, Italy. 

The synthetic polymeric components as well as their combinations with proteins such as human serum albumin (HSA), bovine serum albumin (BSA), human serum albumin/a-interferon mixtures (HSA-IFNa) and myoglobin (MYO) did not give any negative response to in vitro and in vivo biocompatibility tests, such as platelet aggregation, complement activation, acute toxicity, and acute thromboembolic potential. 

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