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At least 217 records · Page 12Linked to original sources
PubMed1993

Bumetanide binding to normal albumins and to albumin in renal failure.

Binding of bumetanide, a loop diuretic, to partially purified albumins from renal failure patients (RF-HA), and healthy subjects (N-HA), human serum albumin (HSA) and defatted-HSA (D-HSA), was studied with equilibrium dialysis at a constant albumin concentration and various ligand concentrations. Binding parameters (n and K) were estimated from Scatchard plots and with a non-linear two-binding site model computer program, assuming two classes of independent sites. The binding capacities (n1K1) decreased in the order N-HA > RF-HA > D-HSA > HSA. Computer estimates of K1 for the partially purified albumin preparations were not markedly different. However, the graphical estimate of K1 for N-HA was greater than that for RF-HA. When the degree of binding (r) was plotted as a function of the logarithm of the free bumetanide concentration, an asymptotic plateau was not observed, indicating that the protein binding sites were not saturated. Consequently, the calculated binding estimates may not adequately describe the binding of bumetanide.

Albumins↗
PubMed2001

The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin.

Although human serum albumin is synthesized without carbohydrate, glycosylated variants of the protein can be found. We have determined the structure of the glycan bound to the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr). The oligosaccharide was released from the protein using anhydrous hydrazine, and its structure was investigated using neuraminidase and a reagent array analysis method, which is based on the use of specific exoglycosidases. The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn. However, a minor part (11 mol%) of the glycan was without sialic acid. The structure is principally the same as that of glycans bound to two other types of glycosylated albumin variants. Glycosylation can affect, for example, the fatty acid binding properties of albumin. Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.

Carbohydrate Sequence↗
PubMed2001

A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.

Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco). The slow-migrating variant and the normal protein were isolated by anion-exchange chromatography and, after treatment with CNBr, the digests were analyzed by two-dimensional electrophoresis in a polyacrylamide gel. The CNBr peptides of the variant were purified by reverse-phase high performance liquid chromatography and submitted to sequence analysis. Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575. DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15. Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure. This oligosaccharide chain has been located to Thr596 by amino-acid sequence analysis of the tryptic fragment 592-597.

Adenine↗
PubMed1970

The termination of immunological unresponsiveness to bovine serum albumin in rabbits. I. Quantitative and qualitative response to cross-reacting albumins.

Rabbits made unresponsive to BSA at birth were given two courses of immunization with various cross-reacting albumins at 3 months of age. Normal control rabbits, of equivalent age and weight, were similarly immunized. Sera obtained 7 days after the last injection were assayed for binding and precipitating antibody to six albumins and for their avidity for BSA. No significant differences were found between unresponsive and normal rabbits in the amount of antibody reacting with any of the six albumins used. This was the case regardless which albumin was used to terminate the unresponsive state. Avidity differences were seen and seemed to depend on the antigen used and not on the immunological status of the animal. The simultaneous injection of small amounts of BSA inhibited the termination of unresponsiveness. These results were discussed in the light of the more recent theories of the termination of unresponsiveness and of antibody formation.

Animals↗
PubMed1977

Quantitative determination of albumin dimer in albumin preparations by combined starch-gel electrophoresis and immunoprecipitation.

A method is described for albumin dimer determination. The method is based upon an electrophoretic separation of albumin dimer from the monomer in starch gel with a subsequent immunochemical diffusion and precipitation of the albumin components in agarose gel containing antibodies. The precipitation zones are measured and compared iwth those of albumin monomer standards. A factor for converting monomer to dimer has furthermore been established.

Albumins↗
PubMed1983

Plasma-to-ascitic fluid transport rate of albumin in patients with decompensated cirrhosis. Relation to intraperitoneal albumin.

Albumin-kinetics and haemodynamic studies were performed in 20 patients with decompensated liver cirrhosis in order to improve the knowledge on genesis and perpetuation of hepatic ascites, especially with respect to determinants of intraperitoneal protein. A positive relationship was found between the plasma-to-peritoneal transport rate of albumin (index of 'lymph-imbalance') and the mass of intraperitoneal albumin (rlog = 0.82, P less than 0.001), indicating a significant role of 'lymph-imbalance' to sequestration of protein in the peritoneal cavity. Ascitic fluid albumin concentration was on the average 0.22 of that of plasma and directly correlated to the plasma concentration (rlin = 0.68, P less than 0.01). The hydrostatic pressure difference across the splanchnic microvasculature (assessed as wedged hepatic vein minus inferior vena caval pressure) was directly correlated to the effective (plasma minus ascitic fluid) oncotic pressure (rlin = 0.74, P less than 0.001) but significantly higher than that (P less than 0.005), indicating a 'non-equilibrium' in the splanchnic Starling forces. The results point to a multivariate genesis and perpetuation of cirrhotic ascites as laid down in the 'lymph-imbalance' theory of ascites formation, whereas a 'fluid equilibrium' theory seems to be too simple, especially with respect to explain protein sequestration in the peritoneal cavity.

Adult↗
PubMed1981

Receptor for albumin on the liver cell surface may mediate uptake of fatty acids and other albumin-bound substances.

Kinetic analysis of the uptake of carbon-14-labeled oleate in a single-pass perfusion of rat liver and saturable and specific binding of iodine-125-labeled albumin to hepatocytes in suspension suggest the existence of a receptor for albumin on the liver cell surface. The putative receptor appears to mediate uptake of albumin-bound fatty acids by the cell and may account for the efficient hepatic extraction of many other substances tightly bound to albumin.

Animals↗
PubMed2003

Novel role for albumin in innate immunity: serum albumin inhibits the growth of Blastomyces dermatitidis yeast form in vitro.

In this study we found that serum inhibitory activity against Blastomyces dermatitidis was principally mediated by albumin. This was confirmed in experiments using albumin from several mammalian species. Analbuminemic rat serum did not inhibit B. dermatitidis growth in vivo; however, the addition of albumin restored inhibitory activity. Inhibitory activity does not require albumin domain III and appears to involve binding of a low-molecular-weight yeast-derived growth factor.

Animals↗
PubMed1979

Evaluation of 99mTc-albumin dilution curve with simultaneous injection of 99mTc- and 131I-albumins.

A critical comparison of radiocardiograms with 99mTc- and 131I-albumins was made to determine whether or not 99mTc-albumin can be used as a tracer for measuring blood volume (BV) and cardiac output (CO). Simultaneous injection of both isotopes was given to twenty-two patients to obtain radiocardiograms for each by means of a single scintillation counter with two pulse height analyzers. Such method allows for the determination of the energy levels for both 99mTc and 131I. The radiocardiographic pattern was somewhat different between 99mTc- and 131I-radiocardiograms: The ratio of left to right peak height was 16% on the average lower in the 99mTc-radiocardiogram in the 131I-one. The reason for the lower ratio is explained by greater absorption of 99mTc-radioactivity within the soft tissue interposing between the scintillation probe and heart. The values for 99mtc-derived blood volume were 7.4% on the average larger than those for 131I-derived blood volume (p less than 0.01), although the correlation was excellent (r = 0.98, p less than 0.01). There was no systemic difference between cardiac output determined by 99mTc- and 131I-albumins since the overstimation of blood volume can compensate for the understimation of CO/BV by 99mTc-study. In view of its rapid extravasation, 99mTc-albumin is not so appropriate tracer for accurate measurements of BV and CO/BV, although it may be used for measurement of cardiac output.

Adolescent↗
PubMed1980

[Evaluation of the functional state of the blood-brain barrier by means of the analysis of total protein, albumin level and albumin index of the cerebrospinal fluid in multiple sclerosis].

A method has been evolved for assessing the functional state of the blood-brain barrier based on determinations of albumin level and calculation from it of the so called albumin index in the cerebrospinal fluid. The results obtained by this method were compared with the value of total protein determination in the assessment of the functional state of the blood-brain barrier with regard to serum proteins. The analysis of these results showed that determinations of the albumin level and albumin index is an objective method in the assessment of the blood-brain barrier. Both methods gave similar results. Determination of the total protein level in the cerebrospinal fluid is of only limited value for the assessment of the functional state of blood-brain barrier in multiple sclerosis.

Albumins↗
PubMed2005

The studies of density, apparent molar volume, and viscosity of bovine serum albumin, egg albumin, and lysozyme in aqueous and RbI, CsI, and DTAB aqueous solutions at 303.15 K.

Density (rho), apparent molar volume (V(phi)), and viscosity (eta) of 0.0010 to 0.0018% (w/v) of bovine serum albumin (BSA), egg albumin, and lysozyme in 0.0002, 0.0004, and 0.0008 M aqueous RbI and CsI, and (dodecyl)(trimethyl)ammonium bromide (DTAB) solutions were obtained. The experimental data were regressed against composition, and constants are used to elucidate the conformational changes in protein molecules. With salt concentration, the density of proteins is found to decrease, and the order of the effect of additives on density is observed as CsI > RbI > DTAB. The trend of apparent molar volume of proteins is found as BSA > egg-albumin > lysozyme for three additives. In general, eta values of BSA remain higher for all compositions of RbI than that of egg-albumin for CsI and DTAB. These orders of the data indicate the strength of intermolecular forces between proteins and salts, and are helpful for understanding the denaturation of proteins.

Animals↗
PubMed1982

Effect of albumin conformation on binding of phenylbutazone and oxyphenbutazone to human serum albumin.

The binding of phenylbutazone (I) and oxyphenbutazone (II) to human serum albumin over pH 6.9-9.3 was studied by difference spectrophotometry and equilibrium dialysis. At each pH tested, there was higher binding affinity of I to human serum albumin than II. Equilibrium dialysis showed that over the pH 7-8.2 range both agents had a single high-affinity site and several sites of lower affinity, with the highest binding constant and number of binding sites at pH 7.4 for both I and II. Both techniques showed that the affinity of both drugs to albumin was higher for the neutral form than for the basic form and this transition occurred in both cases around the neutral region (7-7.4). Both the ionized and unionized forms of I and II participated in the binding. In the neutral region, magnesium ion increased the affinity of both drugs to albumin while chloride ion decreased it slightly.

Chemical Phenomena↗
PubMed1992

Odontogenic tumors in mice carrying albumin-myc and albumin-rats transgenes.

Odontogenic tumors that produce abnormal tooth-like structures are repeatedly observed in mandibles of mice that carry both albumin-myc and albumin-ras transgenes. The earliest lesions appear among the periodontal ligament mesenchymal cells, but later lesions include an epithelial component. Subsequent tumor development recapitulates the process of normal tooth formation, which requires multiple sequential cell signals, and results in cell differentiation, matrix secretion, and mineralization. Tumor cells with epithelial morphology produce ras oncoprotein, consistent with an epithelial origin of these tumors. As albumin regulatory sequences direct oncogene expression in these mice, our findings also suggest that some of the albumin present in normal teeth may be locally produced and have a role in tooth mineral formation. The reproducibility of this phenotype makes these mice an excellent model for studies of both normal and neoplastic odontogenesis.

Animals↗
PubMed1981

Enhancement of the phototherapy effect of albumin in Gunn rats. Investigations on the optimal albumin dose.

In pharmacokinetic studies we proved that the efficacy of phototherapy in jaundiced Gunn rats was enhanced by administration of human albumin. The albumin injections provoked a bilirubin shift from extravascular compartments into the circulation. In this study, calculations on the optimal albumin dose were carried out. After s.c. injections a good effect could be ascertained with doses between 2 and 4 g/kg body weight. After i.v. injections effective plasma concentrations could be maintained for an acceptable time by about 2g albumin/kg body weight. When overdoses were given, a considerable amount of albumin was eliminated very quickly--especially after i.v. injections with the rapid rise of the plasma level. Clinical implications are discussed.

Albumins↗
PubMed2006

Recombinant human serum albumin dimer has high blood circulation activity and low vascular permeability in comparison with native human serum albumin.

PURPOSE: Human serum albumin (HSA) is used clinically as an important plasma expander. Albumin infusion is not recommended for critically ill patients with hypovolemia, burns, or hypoalbuminemia because of the increased leakage of albumin into the extravascular spaces, thereby worsening edema. In the present study, we attempted to overcome this problem by producing a recombinant HSA (rHSA) dimer with decreased vascular permeability and an increased half-life. METHODS: Two molecules of rHSA were genetically fused to produce a recombinant albumin dimer molecule. The pharmacokinetics and biodistribution of the recombinant proteins were evaluated in normal rats and carrageenin-induced paw edema mouse model. RESULTS: The conformational properties of this rHSA dimer were similar to those for the native HSA (the HSA monomer), as evidenced by the Western blot and spectroscopic studies. The biological half-life and area under the plasma concentration-time curve of the rHSA dimer were approximately 1.5 times greater than those of the monomer. Dimerization has also caused a significant decrease in the total body clearance and distribution volume at the steady state of the native HSA. rHSA dimer accumulated to a lesser extent in the liver, skin, muscle, and fat, as compared with the native HSA. Up to 96 h, the vascular permeability of the rHSA dimer was less than that of the native HSA in paw edema mouse models. A prolonged plasma half-life of the rHSA dimer was also observed in the edema model rats. CONCLUSIONS: rHSA dimer has a high retention rate in circulating blood and a lower vascular permeability than that of the native HSA.

Animals↗
PubMed1991

Studies on the carotenoids in the muscle of salmon--V. Combination of astaxanthin and canthaxanthin with bovine serum albumin and egg albumin.

1. Bovine serum albumin (BSA) and/or egg albumin were bound to astaxanthin or canthaxanthin easily and the spectroscopic characteristics of these complexes were similar to those of astaxanthin or canthaxanthin in the salmon muscle. 2. This result indicates that astaxanthin-BSA, -egg albumin, canthaxanthin-BSA and -egg albumin complexes were basically similar to astaxanthin-actomyosin and/or canthaxanthin-actomyosin complex in the salmon muscle. 3. The binding of salmon actomyosin to astaxanthin or canthaxanthin is not specific.

Actomyosin↗
PubMed2006

Determination of plasma thiol bound to albumin using affinity chromatography and high-performance liquid chromatography with fluorescence detection: ratio of cysteinyl albumin as a possible biomarker of oxidative stress.

We examined the influence of oxidative stress on the relative amounts of various albumin-bound thiols in human plasma. To determine the ratio of thiols existing as mixed disulfides following oxidation, we developed a method combining fast purification of albumin using affinity columns and high-performance liquid chromatography (HPLC) with fluorescence detection for low molecular weight thiols which were labeled after reduction. When the effect of exposure of plasma to radical oxygen species on binding of thiols to albumin was determined by the present method, significant increases in the ratio of cysteine bound to albumin (Alb-Cys) to total cysteine were clearly demonstrated.

Adult↗
PubMed1997

Albumin standards and the measurement of serum albumin with bromcresol green. 1971.

A rapid and reliable method for measuring serum albumin employing bromcresol green is described. The addition of albumin to a solution of bromcresol green in a 0.075 M succinate buffer pH 4.20 results in an increase in absorbance at 628 nm. The absorbance-concentration relationship is linear for samples containing up to 6 g/dl albumin. Bilirubin, moderate lipemia, and salicylate do not interfere with the analysis. The use of nonionic surfactant (Brij-35) reduces the absorbance of the blank, prevents turbidity and provides linearity. The results by this method agree very well with those obtained by electrophoresis and salt fractionation. The method is simple, it has excellent precision and the reagents are stable. A protein standard is introduced which can be employed for both the total serum proteins and albumin determinations.

Blood Chemical Analysis↗