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PubMed1984

Binding of [3H]mianserin to bovine serum albumin, human serum albumin and alpha 1-acid glycoprotein.

Scatchard plots which were curvilinear with negative slopes were obtained when the binding of [3H]mianserin to bovine serum albumin (BSA), human serum albumin (HSA), defatted human serum albumin (D-HSA) and alpha 1-acid glycoprotein (alpha 1-AGP) was studied with equilibrium dialysis with constant protein concentrations and various ligand concentrations. Binding parameters were estimated graphically and with a non-linear least-squares computer program, assuming two classes of independent binding sites. alpha 1-AGP had the highest binding affinity (K) and binding capacity (nK). The binding parameters, n and K were not independent of protein concentration when the BSA concentration was varied. Linear atypical Scatchard plots with positive slopes were obtained when the protein concentration was varied for BSA, HSA and D-HSA, at a fixed ligand concentration.

Animals↗
PubMed2000

Implications of the distribution of Albumin Naskapi and Albumin Mexico for new world prehistory.

The known distributions of two mutational variants of the albumin gene that are restricted to Mexico and/or North America, Albumin Mexico (AL*Mexico) and Albumin Naskapi (AL*Naskapi), were expanded by the electrophoretic analysis of sera collected from more than 3, 500 Native Americans representing several dozen tribal groups. With a few exceptions that could be due to recent, isolated cases of admixture, AL*Naskapi is limited to groups that speak Athapaskan and Algonquian, two widely distributed language families not thought to be related, and to several linguistically unrelated groups geographically proximate to its probable ancestral homeland. Similarly, AL*Mexico is limited to groups that speak Yuman or Uto-Aztecan, two language groups in the American Southwest and Baja California not thought to be closely related to each other, and to several linguistically unrelated groups throughout Mexico. The simultaneous consideration of genetic, historical, linguistic, and archaeological evidence suggests that AL*Naskapi probably originated on the northwestern coast of North America, perhaps in some group ancestral to both Athapaskans and Algonquians, and then spread by migration and admixture to contiguous unrelated, or distantly related, tribal groups. AL*Mexico probably originated in Mexico before 3,000 years BP then spread northward along the Tepiman corridor together with cultural influences to several unrelated groups that participated in the Hohokam culture.

Albumins↗
PubMed1994

Aminoguanidine reduces regional albumin clearance but not urinary albumin excretion in streptozotocin-diabetic rats.

Advanced glycation end-product-formation is thought to play a role in the development of diabetic angiopathy. By altering the structure of different extracellular matrix components advanced glycation end-products might affect vascular and glomerular permeability. In this study we investigated the effect of treatment with an inhibitor of advanced glycation end-product-formation, aminoguanidine, on vascular permeability and the development of albuminuria in streptozotocin-induced diabetic rats. Male Wistar Rp rats were randomized into a control group, a diabetic group, and an aminoguanidine-treated diabetic group. After 8 weeks, 24-h urine collections were taken and rats were implanted with an arterial and a venous catheter. mean arterial blood pressure was determined by intra-arterial measurement. Regional albumin clearances were assessed in the eye, ileum, lung, skeletal muscle and skin using an isotope technique. Mean arterial pressure in the diabetic group was significantly lower in the control and aminoguanidine-treated groups (p < 0.02). Regional albumin clearances were significantly increased in all tissues of diabetic rats compared to control rats (p < 0.05). Aminoguanidine treatment of diabetic rats resulted in a significant decrease of regional albumin clearance in all tissues except the lung (p < 0.05, lung p = 0.07). The development of albuminuria in diabetic rats however, was not affected by aminoguanidine.

Albuminuria↗
PubMed1977

Modification of the binding of sulphamidochlorobenzoic acid to human albumin by palmitic acid contamination of albumin.

Palmitic acid a common contaminant of albumin preparations, competitively inhibits the binding of sulphamidochlorobenzoicacid (SCBA) to human albumin thus decreasing its observed affinity. The effect of palmitic acid depends on its concentration, i.e. the purity and concentration of the albumin preparation used. The correct value for SCBA affinity was obtained by correcting the experimental data according to the palmitic acid concentration by use of a multiligand analysis method.

Albumins↗
PubMed1994

Isolation and characterization of sets of anti-L-fucose and anti-bovine serum albumin antibodies directed against a glycoconjugate of L-fucose and bovine serum albumin.

A set of anti-carbohydrate antibodies and a set of anti-protein antibodies were isolated from the serum of rabbits immunized with a glycoconjugate of L-fucose and bovine serum albumin. The sets were separated by affinity chromatography by a two-column method on adsorbents with L-fucose or bovine serum albumin ligands. Isoelectrofocusing results showed that the anti-carbohydrate antibodies consisted of 11 molecular species and the anti-bovine serum albumin antibodies consisted of seven molecular species. The anti-carbohydrate antibodies are all of the IgG type while the anti-protein antibodies contain three types of globulin molecules, IgA, IgG, and IgM. The former antibodies should be useful as markers for unique glycoproteins of diseased cells and the latter antibodies may be useful for investigating the mechanism of simultaneous synthesis of three types of immunoglobulins.

Animals↗
PubMed1983

Positive cooperativity in binding by albumin: the system bovine serum albumin and alizarin yellow G cobinding by salicylic acid.

The binding of alizarin yellow G--an azo derivative of salicylic acid--by bovine serum albumin has been investigated using the method of equilibrium dialysis. Six strong and a number of additional, weak binding sites have been found to be present. The system is characterized by strong positive cooperativity between the first and second sites. Six binding constants have been determined on the basis of a simplified mathematical model. The results are approximately 2 X 10(4) M-1 for the first binding site, 6 X 10(5) M-1 for the second, and between 4 X 10(4) and 10(5) M-1 for the rest. The phenomenon is discussed in terms of the existence of various conformers or of the conformational adaptability of albumin. Cobinding by salicylic acid does not displace alizarin yellow G but induces a conformational change in the protein which affects the absorption spectrum of the bound dye. As expected for this kind of heterotropic interaction, the spectrum of the system albumin-salicylic acid is similarly affected by the cobinding of alizarin yellow G.

Animals↗
PubMed1998

Indirect immobilization of recombinant proteins to a solid phase using the albumin binding domain of streptococcal protein G and immobilized albumin.

Immobilization of proteins to a solid phase leads to denaturation of the adsorbed molecules which may subsequently affect biological interactions. However, for many applications maintenance of the native structure is desired. Therefore, an indirect immobilization system was developed, based on binding of the albumin binding domain (ABP) of streptococcal protein G to rat serum albumin (RSA) precoated on a solid phase (RSA-microtiter plates). Escherichia coli vectors were adapted for production of recombinant protein fused to ABP and the 6 X His-tag. The expressed ABP tag was found to form homodimers. Plasmon resonance was used to study the interaction between an ABP fusion protein and immobilized RSA. Apparent on- and off-rates were calculated using a model for a bivalent analyte (k(a1) = 3.37 x 10(4) M(-1) s(-1), k(d1) = 1.23 x 10(-4) s(-1)). Thus, the stability of the ABP-RSA interaction can be explained by a slow off-rate. This was confirmed by chase experiments in an ELISA format. The ABP-RSA interaction remained stable after addition of different albumins. This immobilization system was used for the development of an ELISA to detect antibodies against Borna disease virus protein p40. The use of RSA-microtiter plates for indirect immobilization of ABP fusion protein was shown to be superior to direct adsorption on plastic. To obtain maximal antibody binding ten times less antigen was needed for indirect immobilization compared to direct adsorption. The binding capacity of the RSA-microtiter plates was determined to be about 0.8 pmol of monomeric ABP protein.

Adsorption↗
PubMed1990

High-performance liquid chromatographic determination of the binding of ceftriaxone to human serum albumin solution and albumin from diluted human serum.

The binding of ceftriaxone to human serum albumin has been studied by high-performance liquid chromatography. The gel permeation method of Hummel and Dreyer was used. Ceftriaxone was tested with two sources of albumin (aqueous solution and diluted serum). After internal calibration the binding parameters were determined for each albumin, and results compared. These data are in agreement with those from classical methods for the determination of protein binding of ceftriaxone.

Buffers↗
PubMed1975

Chemical structure of two fragments of human serum albumin and their location in the albumin molecule.

1. 'Inhibitor fragment' isolated from human serum albumin degraded by rabbit cathepsin D is composed of one peptide chain with two intrachain disulphide bonds. There are two kinds of inhibitor molecules having different N-terminal amino acids: one is threonine and the other glutamine. 2. Fragment F1, isolated from inhibitor degraded by trypsin, is composed of two chains linked by a disulphide bond. There are three kinds of fragment F1. All have one alpha chain in common, which has an intrachain disulphide bond. They differ by the nature of the chain, which is linked to the alpha chain by a disulphide bond. The epsilon chain is present in trace amounts. The two other chains, beta and gamma, differ by their C-terminal amino acid, which is respectively arginine and lysine. 3. Inhibitor is composed of the last 92 or 89 residues of the human albumin molecule and fragment F1 is composed of two parts of this C-terminal portion of the albumin molecule.

Alkylation↗
PubMed2002

Mutational analysis of the interaction between albumin-binding domain from streptococcal protein G and human serum albumin.

Streptococcal protein G (SpG) is a bacterial cell surface receptor exhibiting affinity to both human immunoglobulin (IgG) and human serum albumin (HSA). Interestingly, the serum albumin and immunoglobulin-binding activities have been shown to reside at functionally and structurally separated receptor domains. The binding domain of the HSA-binding part has been shown to be a 46-residue triple alpha-helical structure, but the binding site to HSA has not yet been determined. Here, we have investigated the precise binding region of this bacterial receptor by protein engineering applying an alanine-scanning procedure followed by binding studies by surface plasmon resonance (SPR). The secondary structure as well as the HSA binding of the resulting albumin-binding domain (ABD) variants were analyzed using circular dichroism (CD) and affinity blotting. The analysis shows that the HSA binding involves residues mainly in the second alpha-helix.

Bacterial Proteins↗
PubMed1977

Horizontal polyacrylamide gradient gel electrophoresis for the simultaneous phenotyping of transferrin, post-transferrin, albumin and post-albumin in the blood plasma of cattle.

A simple method of horizontal polyacrylamide gel electrophoresis was described for the simultaneous phenotyping of transferrin, post-transferrin, albumin and post-albumin in the blood plasma of cattle. A step gradient gel of 8, 4, 12 and 14% acrylamide concentration was used. The method enabled the detection of a new protein polymorphism in the post-transferrin region. Two alleles were observed. The transferrin phenotypes involving D1 and D2 alleles were clearly separated. The resolution of the post-albumin fractions was also better than described by earlier methods.

Alleles↗
PubMed1993

Dialysis against a recycled albumin solution enables the removal of albumin-bound toxins.

The removal of protein-bound substances of pathogenetic relevance from blood is of therapeutic interest for drug intoxications, renal and liver failure, and metabolic disorders. Current methods using adsorbents are effective but often not specific enough. This work presents an alternative method that enables the dialyzability of albumin-bound toxins from plasma by the use of a high-flux dialyzer (F 60 Fresenius) and an albumin solution circulating on the dialysate side to increase selectively the affinity for albumin-bound toxins. This method resulted in effective removal of unconjugated bilirubin, drugs with a high protein-binding ratio (sulfobromophthalein, theophylline), and a protein-bound toxin (phenol). The additional removal of PBS could extend the applicability of dialysis, for example, to drug intoxications and liver failure or could improve the elimination of protein-bound uremic toxins in chronic renal failure.

Adsorption↗
PubMed1986

Human antibodies against formaldehyde-human serum albumin conjugates or human serum albumin in individuals exposed to formaldehyde.

Sera from patients undergoing hemodialysis with formaldehyde (F)-sterilized dialyzers were studied to determine if antibodies against F conjugated to human serum albumin (HSA) could be detected. F-human serum albumin (F-HSA) conjugates were prepared using ratios of F to HSA that did not precipitate the HSA. The F-HSA conjugates migrate differently electrophoretically than HSA with an increased negative charge of F-HSA as compared with HSA. The F-HSA was used in an ELISA. The results demonstrated that in certain sera, IgG, IgM, IgA and IgE antibodies against F-HSA could be measured. In the highest titered sera, it was shown that the IgG antibody was not directed against F alone or F-lysine but against an antigenic grouping of F-HSA. No correlation of either IgG or IgE antibodies with immune complex or allergic reactions was found in this series of dialysis patients. Some sera from dialysis patients had antibody activity against HSA. Sera from 2 physicians with rhinitis after F exposure had no antibody activity against F-HSA or HSA. Two nurses with a history of F-induced asthma had no IgG antibodies but did have IgE antibodies against F-HSA and HSA. This spectrum of immunologic responses is analogous to responses in dogs immunized with F or F dog albumin. We have not been able to identify anti HSA antibodies in patients reactive to other hapten-HSA compounds and it is suggested that anti HSA antibodies in F-exposed humans may relate to the F exposure.

Antibody Specificity↗
PubMed1986

Characterization of the interaction of albumin with isolated rat liver cells to reveal the mechanism of albumin-mediated hepatic transport.

The binding of bovine serum albumin (BSA), containing 125I-BSA, to isolated rat hepatocytes was studied over a 300-fold concentration range of BSA to characterize the interaction between albumin and the liver cells in albumin-mediated hepatic transport. The binding of BSA with a high affinity to the cell surface of hepatocytes was not found in the binding behavior. The bound fraction of BSA with hepatocytes was about 1% over those concentration range of BSA.

Animals↗
PubMed1991

Human serum albumin inhibits prostacyclin production by endothelial cells: the relation of the inhibitory activity to sulfhydryl groups in albumin.

Human serum inhibited calcium ionophore-induced production of prostacyclin by cultured bovine aortic endothelial cells. The inhibitory fraction was purified from serum by anion-exchange and Blue-Sepharose affinity chromatography. The molecular weight of the purified substance was 67k dalton as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It was identified as human serum albumin by N-terminal amino acid sequence analysis. Human serum albumin was separated to two forms by high-performance liquid chromatography: mercaptalbumin (SH type) and nonmercaptalbumin (SS type). Both types of albumin inhibited the conversion of arachidonic acid to prostaglandin H2 in a dose-dependent manner without affecting phospholipase A2 or prostacyclin synthetase. This inhibition was more potent in mercaptalbumin than in nonmercaptalbumin. These results suggest that the conversion between mercaptalbumin and nonmercaptalbumin may play an important role in the modulation of prostacyclin synthesis by endothelial cells.

Adenosine Diphosphate↗
PubMedDate not supplied

[Study of the amino acid composition of albumin fractions obtained from human serum albumin].

Six fractions were isolated from the commercial lyophised albumin preparation by the method of deposition in the medium of 3M KCl. The fractions were purified by means of preparative disc electrophoresis from globulins and polymers, and their amino acid composition was studied on the analyser KLA-3B. The significant differences (p=0.001) are found by lysine, ammonia, histidine, arginine, threonine, glutaminic acid, and phenyl alanine. The greatest differences are found by lysine, ammonia, glutaminic acid and phenylalanine. The fraction was also found being 9% of the initial albumin and sharply differing from the rest of the fractions in amino acid composition but identical immunologically. It is supposed that albumin heterogeneity is connected both with the presence of molecular forms differing in the primary structure and with different degree of amidation of glutaminic and aspartyl residues.

Amino Acids↗
PubMed1979

Gallium-68 labeling of albumin and albumin microspheres.

Because of the high stability constant of gallium transferrin, the formation of a protein that will be stable in vivo and labeled with gallium-68 (a positron emitter) requires preliminary coupling of a strong chelating group to the protein. In the present study, we have used a reaction developed by Krejcarek and Tucker, in which DTPA is coupled to proteins by the formation of an amide bond. Using human serum albumin (HSA) as a model, we have studied the efficiency of the reaction of HSA with the mixed acid anhydride of the quarternary triethyl ammonium salt of DTPA and butyl formate, as a function of the ratio of albumin to DTPA. After purification of the DTPA-labeled HSA, it is possible to prepare Ga-68-labeled albumin in high yield by chelation of the Ga-68 with the DTPA-labeled protein. In vitro and in vivo stability studies showed that the labeled protein was stable over a period of several hours. The same type of bifunctional chelate has been used to attach Ga-68 to HSA microspheres.

Animals↗
PubMed1981

The evolution of alpha-fetoprotein and albumin. II. The structures of the alpha-fetoprotein and albumin genes in the mouse.

The murine alpha-fetoprotein (AFP) and albumin genes have been cloned from genomic libraries derived from Balb/c DNA. By restriction endonuclease mapping and electron microscopy, we have shown that both genes are organized similarly into 15 coding segments interrupted by 14 intervening sequences. The sizes of the corresponding coding segments in each gene are identical, lending support to the hypothesis that the two genes, were derived from a common ancestral gene. However, no nucleotide homology between coding segments was observed. Both the sizes and the nucleotide sequence of flanking and intervening sequences have diverged significantly as well. Two regions of the AFP gene, 925 base pairs in the 5' flanking DNA and 180 base pairs in the third intervening sequence, hybridized to the same region of DNA in the third intervening sequence of albumin. The 180-base pair homologies within each gene are present in opposite orientation relative to the direction of transcription, and are associated with reiterated DNA. Thus, it is unlikely that they represent true sequence conservation. An examination of the sizes of the coding segments in each gene reveals a thrice repeated domain, consisting of 4 coding segments. We propose that these correspond to the three domains observed in several mammalian albumins, and in murine AFP.

Albumins↗