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At least 343 records · Page 19Linked to original sources
PubMed1989

Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family.

The Xenopus laevis 68-kd and 74-kd albumin amino acid sequences are examined with respect to their relationship to the other known members of the albumin/alpha-fetoprotein/vitamin D-binding protein gene family. Each of the three members of this family presents a unique pattern of conserved regions indicating a differential selective pressure related to specific functional characteristics. Furthermore, an evolutionary tree of these genes was deduced from the divergence times calculated from direct nucleotide sequence comparisons of individual gene pairs. These calculations indicate that the vitamin D-binding protein/albumin separation occurred 560-600 million years (Myr) ago and the albumin/alpha-fetoprotein divergence 280 Myr ago. This observation leads to the hypothesis according to which the albumin/alpha-fetoprotein gene duplication occurred shortly after the amphibian/reptile separation. Consequently, and unlike mammals, amphibians and fishes should lack an alpha-fetoprotein in their serum at larval stages, which is consistent with a recent analysis of serum proteins in Xenopus laevis larvae. This hypothesis now will have to be tested further in additional lower vertebrates.

Albumins↗
PubMed1992

Albumin binding in uraemia: quantitative assessment of inhibition by endogenous ligands and carbamylation of albumin.

The binding capacity of human serum albumin (HSA) for small acidic molecules is known to be reduced in chronic renal failure (CRF). The contribution of competitive inhibition by accumulated endogenous ligands and of structural changes in HSA has now been evaluated. In a fluorimetric in vitro assay using HSA and two dansylated amino acids the inhibitory properties of various endogenous ligands were determined in concentration-effect studies. The effect of carbamylation of HSA on binding was also examined. The mode of inhibition, including binding parameters n and Ka, was determined. Finally, HSA binding in sera from controls and dialysis patients was compared in a modified assay. Thirty three substances were tested and were placed in 3 groups: strong inhibitors (IC50 < 3*10(-5) mol.l-1, e.g. indolyl acids, furanoic acids), medium inhibitors (IC50 > 3*10(-5), eg. vanillic acid), and no inhibition (e.g. urea, creatinine, guanidino compounds). Complete (> 80%) carbamylation of HSA reduced binding by 67% in a non-competitive mode. There was a significant reduction in the binding capacity of HSA from the dialysis patients (approximately 24%), irrespective of medication. It is concluded that the uraemic binding defect of HSA is caused by competitive inhibition by the many physiological ligands accumulated in CRF and structural modifications of HSA. The assay presented proved useful for the rapid analysis of possible HSA binding inhibitors and for testing large groups of patients, e.g. comparison of dialysis treatments, and pharmacological binding studies.

Amino Acid Sequence↗
PubMed1992

Exchange efflux of [3H]palmitate from human red cell ghosts to bovine serum albumin in buffer. Effects of medium volume and concentration of bovine serum albumin.

[3H]Palmitate, PA, exchange efflux kinetics is recorded from human erythrocyte ghosts to buffer with bovine serum albumin, BSA, at 0 degrees C. The effects have been investigated of three medium/ghost volume ratios: 36, 80 and 500, of six BSA concentrations, [BSA]: 0.01, 0.02, 0.05, 0.2, 1 and 2% (1.5, 3.0, 7.5, 30, 150 and 300 microM) and of various v, molar ratios of palmitate to BSA, between 0.15 and 0.94. Data are analyzed in terms of a virtually closed three-compartment model. In theory, the tracer efflux is biexponential and the rate coefficients differ at least 20 fold [1]. The efflux rate at 2% BSA is monoexponential beyond our resolution time of about 1 s, but nearly biexponential at or below 0.2% BSA with a well-defined smallest-rate coefficient beta. beta depends strongly on [BSA] but is remarkably v independent. The medium/ghost volume ratio has no effect on beta when [BSA] > or = 0.2%, although beta measured at 2% BSA is almost 2-fold higher than at 0.2%. This suggests the presence of an unstirred layer, USL. According to our model, the observations are understood quantitatively on basis of our previously published dissociation rate constants of the PA-BSA complex, as well as PA equilibrium bindings to ghost membranes (Bojesen, I.N. and Bojesen, E. (1991) Biochim. Biophys. Acta 1069, 297-307). Essentially, beta is theoretically a function of two terms, one comprising the membrane transport parameters and the other the medium-dependent variables. Most important is the clearance with respect to monomer concentration adjacent to the membrane. The clearance is calculated on basis of quasi-stationary diffusion in USL. The data are compatible with a planar USL of 6 microns depth and with the same area as a ghost but not with a spherical USL.

Animals↗
PubMed1995

Characterization of thyroxine-albumin binding using high-performance affinity chromatography. II. Comparison of the binding of thyroxine, triiodothyronines and related compounds at the warfarin and indole sites of human serum albumin.

High-performance affinity chromatography was used to examine the binding of thyroid hormones and related compounds at the warfarin and indole sites of human serum albumin (HSA). This was studied by continuously applying L-triiodothyronine (L-T3), L-reverse triiodothyronine (L-rT3) or structural analogs of these compounds to an immobilized HSA column while making injections of site-specific probe molecules (i.e. R-warfarin and L-tryptophan). The results were compared with those obtained previously for L-thyroxine (L-T4). Equilibrium association constants and thermodynamic parameters measured by this approach showed good agreement with previous models reported for L-T4 and L-T3 at their high-affinity sites on HSA. This data confirmed that the phenol groups of L-T4 and L-T3 played a significant role in the binding of these compounds at the indole site. Work performed at the warfarin site and with other solutes (e.g. L-rT3) indicated that additional factors, such as interactions through the thyronine backbone or terminal amine and carboxyl groups of these compounds, could also be involved in the binding of thyroid hormones to HSA.

Binding Sites↗
PubMed1995

Separation of lipoproteins, albumin and gamma-globulin by single-step ultracentrifugation of human serum. Application. I: Binding of hematoporphyrin to human serum and to albumin.

Previous studies of the serum binding of the photosensitizer hematoporphyrin (Hp) have given widely different results. The serum binding of Hp is therefore further illuminated by experiment and discussion. Ultracentrifugal separation of serum is improved and applied to study the binding of Hp to human serum and HSA. The observed distribution of Hp among the serum proteins is compared with the distribution expected from available association constants for Hp binding with individual proteins. The lipoprotein classes and the two major high density proteins (HDP), albumin and gamma-globulin, were separated in a NaCl-KBr gradient by single spin ultracentrifugation (SW 40; 30,000 rpm). HSA- and HDP-bound Hp were similarly distributed in the centrifuged gradient. Centrifugation of Hp-doped HSA separated the unbound Hp (75%) and the HSA-bound Hp (25%). The present association constant for the Hp-HSA complex (10(3)/M) was much lower than earlier published ones (10(6)/M) found by other techniques. The association of Hp with HDP in serum was much stronger than the association of Hp with the isolated HSA (electrophoretic grade). The estimated ratio of HSA-bound to LDL-bound HP in serum was at least 25 times larger than the experimental value. The percentage of LDL-bound Hp decreased with increasing Hp concentration. The serum binding of Hp is the same as that found previously using another rotor and another salt gradient (70.1 Ti, 70,000 rpm, NaCl-CsCl). LDL has high-affinity-low-capacity binding sites for Hp. HSA is the major HDP protein that binds Hp in human serum. The strength of the HSA-Hp complex may depend on the batch of HSA used and upon the absence/presence of other proteins. Proteins may interact in serum in manners that affect the binding of certain drugs. Neither the type of gradient salt nor the field of gravity affected the serum binding of Hp.

Blood Proteins↗
PubMed2004

Stabilizing mechanisms in commercial albumin preparations: octanoate and N-acetyl-L-tryptophanate protect human serum albumin against heat and oxidative stress.

The capability of octanoate, N-acetyl-L-tryptophanate (N-AcTrp) and other ions of fatty acids and amino acids to stabilize human serum albumin (HSA) against thermal and oxidative stress was studied. Native-PAGE showed that octanoate, and more hydrophobic fatty acids anions, stabilizes the monomeric form of HSA during heating at 60 degrees C for 30 min. Heating in the presence of octanoate did not change the far-UV CD-spectrum. The stabilizing role of octanoate also showed as an increase in denaturation temperature and calorimetric enthalpy, determined by differential scanning calorimetry (DSC). N-AcTrp, which was found to compete with octanoate for a common high-affinity site, has only a minor stabilizing effect. By contrast, no effect was found for l-tryptophanate or N-acetyl-L-cysteinate. Any ligand effect on oxidation was examined by using 2,2' -azobis(2-amidino-propane)dihydrochloride (AAPH) as oxidizing agent. One hour of incubation resulted in the formation of the same number of carbonyl groups, whether octanoate or one of the above mentioned amino acids was present or not. However, the number of groups formed after 24 h of incubation was significantly decreased in the presence of L-tryptophanate and, especially, N-AcTrp. The effect of 1-h incubation with AAPH on the oxidative status of 34-Cys was studied by the HPLC technique. It was found that N-AcTrp, but not octanoate, has a large protecting effect on the sulfhydryl group. Thus, octanoate has the greatest stabilizing effect against heat, whereas the presence of N-AcTrp diminishes oxidation of HSA.

Calorimetry, Differential Scanning↗
PubMed2005

IgG antibodies against bovine serum albumin in humans--their prevalence and response to exposure to bovine serum albumin.

Human exposure to bovine serum albumin (BSA) is very common and occurs through dietary and medicinal routes. Although great effort has been made to reduce exposure to BSA in pharmaceuticals to eliminate the threat of bovine spongiform encephalopathy, less attention has been given to assessing the human immune response after exposure to BSA. A sensitive quantitative radioimmunoassay was therefore developed to measure anti-BSA IgG antibodies in healthy subjects and in cancer patients participating in a randomized, placebo controlled clinical trial where they were exposed to BSA as an intrathoracic surgical sealant during pneumonectomy. Anti-BSA antibodies were detected in 55% of 60 healthy blood donors and 51% of 83 patients before lung cancer resection. The median antibody levels were the same in both cohorts; 0.086 microg/mL (range 0.016-19.5 microg/mL) for health blood donors and 0.062 microg/mL (range 0.009-44 microg/mL) for cancer patients. Six months after exposure of the cancer patients to BSA, the percentage of patients with anti-BSA antibody rose to 96% and the median antibody level rose to 19 microg/mL (range 0.009-258 microg/mL). Placebo-treated cancer patients showed no significant increase in the percentage of patients with anti-BSA antibody (41%) or the median antibody level (0.047 microg/mL; range 0.008-1.58) over 6 months. Western blot analysis confirmed the presence of anti-BSA antibody. Elevated levels of anti-BSA antibody were not associated with any detectable clinical events in either the healthy blood donors or the cancer patients.

Animals↗
PubMed2006

Effect of human serum albumin on drug metabolism: structural evidence of esterase activity of human serum albumin.

Human serum albumin (HSA) is the most abundant plasma protein in the human body with a plasma concentration of 0.6mM. HSA plays an important role in drug transport and metabolism. Enzymatic activity of HSA on different substrates or drugs has been studied and documented. The structural mechanism of this activity, however, is unknown. In this study, we have determined the crystal structures of HSA-myristate in a complex of aspirin and of salicylic acid, respectively. The crystal structure of HSA-myristate-aspirin illustrates that aspirin transfers acetyl group to Lys199 and is hydrolyzed into salicylic acid by HSA. The hydrolysis product, salicylic acid, remains bound to HSA at a similar location, but it shows a very different orientation when compared with the salicylic acid in the HSA-myristate-salicylic acid ternary complex. These results not only provide the structural evidence of esterase activity of HSA, and demonstrate the conformational plasticity of HSA on drug binding, but also may provide structural information for the modulation of HSA-drug interaction by computational approach based on HSA-drug structure.

Aspirin↗
PubMed1998

Genetic variation in human serum albumin: a 313 Lys-->Asn mutation in albumin reading identified by PCR analysis.

An early case of bisalbuminaemia was reported in this journal in 1964, with the name Albumin Reading added later. Its use in electrophoretic comparisons led to some new variants being described as 'of the Reading type' on this basis alone. Protein sequencing and DNA studies have since found the single point mutation 313 Lys-->Asn common to this type, but the eponymous variant has not, until recently, been available for study. We now report on its characterisation using PCR analysis with allele-specific oligonucleotide primers, a method also applicable to studies of the population distribution of variants. We also draw attention to the need to link clinically-significant effects to individual variants of known structure.

Aged↗
PubMed1979

Equilibrium saturation chromatographic method for studying the binding of ligands to human serum albumin by high-performance liquid chromatography. Influence of fatty acids and sodium dodecyl sulphate on warfarin-human serum albumin binding.

A size exclusion chromatographic method for studying ligand-macromolecule binding parameters is described. This equilibrium saturation method allows the determination of the concentrations of constituents in equilibrium and is specially useful for characterizing ligand--protein binding under conditions that can be compared with physiological conditions. The method has been used for measuring warfarin--human serum albumin (HSA) binding and for studying the influence of free fatty acids (FFA) and sodium dodecyl sulphate on warfarin--HSA binding. Some comparisons with the Hummel and Dreyer method are given. The influence of the FFA is strongly dependent on their chain length, with an inversion of the effect for a 10-carbon chain.

Chromatography, High Pressure Liquid↗
PubMed2000

Biosensor analysis of the interaction between immobilized human serum albumin and drug compounds for prediction of human serum albumin binding levels.

The interactions between a set of drugs, selected on the basis of reported human serum albumin (HSA) binding levels, and immobilized HSA were investigated using surface plasmon resonance technology. Major HSA binding sites were available after immobilization. The intensity of the signal obtained from the interaction of the drug with the HSA surface was correlated with the reported HSA binding level. Drugs were classified into groups corresponding to high, medium, or low HSA binding based on the injection of the drug at 80 microM concentration. A set of 10 drugs binding to alpha(1)-acid glycoprotein (AGP) was also investigated and correlated with reported AGP binding data. The throughput of the presented assay is 100 compounds/24 h, and the sample consumption is less than 100 microL (8 nmol).

Binding Sites↗
PubMed2000

Stability of human serum albumin during bioprocessing: denaturation and aggregation during processing of albumin paste.

PURPOSE: To assess the impact of various bioprocessing steps on the stability of freshly precipitated human serum albumin (HSA) obtained from pooled human plasma. METHODS: After initial precipitation of HSA from plasma, the resultant paste is either (a) lyophilized or (b) washed with acetone and then air-dried in order to obtain a dry powder. The structure of HSA was examined using Fourier transform infrared (IR) spectroscopy. The extent of aggregation of redissolved HSA was measured using both dynamic light scattering and SDS-polyacrylamide gel electrophoresis (SDS-PAGE). RESULTS: Both lyophilization and air-drying perturb the secondary structural composition of HSA, as detected by infrared (IR) spectroscopy. Upon dissolution of dried paste, most of the protein refolds to a native-like conformation. However, a small fraction of the protein molecules form soluble aggregates that can be detected by both dynamic light scattering and SDS-PAGE. The level of aggregation is so low that it could not be detected in the bulk by either circular dichroism or IR spectroscopy. The lyophilized protein, which appears to be more unfolded in the solid state than the acetone washed/air-dried material, exhibits a higher level of aggregation upon dissolution. CONCLUSIONS: There is a direct correlation between the extent of unfolding in the solid state and the amount of soluble aggregate present after dissolution. Moreover, the presence of the aggregates persists throughout the remainder of the purification process, which includes dissolution, chromatography, sterile filtration and viral inactivation steps. Analytical methods used to monitor the stability of biopharmaceuticals in the final product can be used to assess damage inflicted during processing of protein pharmaceuticals.

Freeze Drying↗
PubMed2003

Albumin dialysis in cirrhosis with superimposed acute liver injury: possible impact of albumin dialysis on hospitalization costs.

Albumin dialysis using the Molecular Adsorbents Recirculating System (MARS) has been found to be beneficial in the treatment of cirrhotic patients with acute decompensation to improve survival as well as reduce associated complications. The present study attempts to analyze the costs involved, and compare it to the benefit as a result of the MARS therapy, thus evaluating its cost-effectiveness. Using the results of a study by Kim et al. describing the effects of complications on the cost of hospitalization in alcoholic liver disease patients, the expenditure incurred in a group of 11 patients treated with standard medical therapy (five survivors) and a group of 12 patients treated with MARS in addition (11 survivors) (Heemann et al., Hepatology 2002) were analyzed. MARS resulted in a reduction of in-hospital deaths, as well as liver disease-related complications. Both these factors led to a substantial reduction of costs in the MARS group, which was enough to counterbalance the extra costs associated with extra-corporeal therapy. In the control group, the total hospitalization cost per survivor were calculated to be at $35,904. In the MARS group, the overall expenditure per survivor including standard medical therapy plus additional MARS liver support therapy were $32,036--a saving of nearly $4000 compared to the control group. Therefore, it appears that the benefits of MARS therapy are enough to justify the cost of treatment and safe hospital costs, at least in the described population. However, further studies are needed to confirm these results.

Albumins↗
PubMed2002

Review article: albumin as a drug--biological effects of albumin unrelated to oncotic pressure.

Albumin is the main determinant of plasma oncotic pressure and it plays a pivotal role in modulating the distribution of fluids between compartments. Moreover, it has many other biological properties which may be important not only for its physiological actions but also for its therapeutic effects. Among the non-oncotic properties are its capacity of molecule transportation and free radical scavenging, its ability to modulate capillar permeability, neutrophil adhesion and activation and its haemostatic effects. The following article reviews these biological effects as well as its structure, synthesis, catabolism and distribution.

Anti-Inflammatory Agents, Non-Steroidal↗
PubMed1992

Design of yeast-secreted albumin derivatives for human therapy: biological and antiviral properties of a serum albumin-CD4 genetic conjugate.

Due to its remarkably long half-life, together with its wide in vivo distribution and its lack of enzymatic or immunological functions, human serum albumin (HSA) represents an optimal carrier for therapeutic peptides/proteins aimed at interacting with cellular or molecular components of the vascular and interstitial compartments. As an example, we designed a genetically engineered HSA-CD4 hybrid aimed at specifically blocking the entry of the human immunodeficiency virus into CD4+ cells. In contrast with CD4, HSA-CD4 is correctly processed and efficiently secreted by Kluyveromyces yeasts. In addition, its CD4 moiety exhibits binding and antiviral in vitro properties similar to those of soluble CD4. Finally, the elimination half-life of HSA-CD4 in a rabbit experimental model is comparable to that of control HSA and 140-fold higher than that of soluble CD4. These results indicate that the genetic fusion of bioactive peptides to HSA is a plausible approach toward the design and recovery of secreted therapeutic HSA derivatives with appropriate pharmacokinetic properties.

Animals↗
PubMed1972

Immune responses against native and chemically modified albumins in mice. I. Analysis of non-thymus-processed (B) and thymus-processed (T) cell responses against methylated bovine serum albumin.

Immune cells induced by bovine serum albumin (BSA) and its methylated derivative (MBSA) have been compared in a cooperative cell transfer system for their content of BSA-specific antibody-forming cell precursors (AFCP, B) and BSA-specific helper (T) cells. When MBSA immune cells were transferred together with hapten-primed cells into recipient mice which were stimulated by a hapten-BSA conjugate, their cooperative secondary anti-hapten response was as good as in case of transferred BSA immune cells. Their secondary anti-BSA response, however, was markedly reduced (reduction factor > 30). Hapten-MBSA conjugates had the same capacity to react with BSA-specific helper cells in the cooperative secondary anti-hapten response as hapten-BSA conjugates but had a reduced ability to react with BSA-specific AFCP cells. In spite of the pronounced reduction of the B cell response, MBSA had the same threshold dose as BSA for activating BSA-specific T cells. These data suggest that B and T cells recognize different epitopes on the BSA molecule, only those recognized by B cells being affected by the methylation procedure.

Animals↗
PubMed1977

A human albumin of placental origin (albumin Rhodia) tested for tolerance.

Fifty infusions, each containing 125 ml 20% human albumin extracted from placental tissue, were tested in clinical practice. No effects such as changes in the patient's BP, pulse rate and rectal temperature were noted during the observation period, and no side-effects such as pain, dyspnoea, nasal symptoms, exanthema or thrombophlebitis, nor any other symptoms to suggest that the solution was not well tolerated.

Adult↗
PubMed1986

Regulation of the immune response to hepatitis B virus and human serum albumin. I. Hepatitis B surface antigen-induced secretion of antibodies with specificity for human serum albumin in hepatitis B-immune donors in vitro.

The circulatory pool of B cells, from donors immune to hepatitis B (HB) through natural infection, contained sensitized B cells with the capacity to secrete antibodies with specificity for human serum albumin (HSA) when stimulated with purified hepatitis B surface antigen (HBsAg) in vitro. The immunoglobulin secretion was dependent upon and regulated by T cells and specifically induced, since it was not obtained in cell cultures from HB-susceptible donors. Culture supernatants with anti-HSA reactivity also contained specific antibodies to HBsAg (anti-HBs), indicating that the outer coat of HBV normally provokes an immune response to both the viral antigen and a 'self' component. Perturbation in the regulation of the immune response triggered by HSA in association with HBV/HBsAg particles may involve a putative risk for development of chronic HBsAg carriership.

Antibody Specificity↗