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PubMed1983

C1q has albumin binding activity but does not interfere in the hemagglutination test for anti-albumin antibodies.

Two factors in the sera of patients with liver disease interact with polymerized human serum albumin (HSAP). These are anti-albumin antibodies (AAA) and receptors for polymerized albumin on HBsAg. Recently it was demonstrated by radioimmunoassay that purified human C1q also binds HSAP. Our data confirm the reaction between purified human C1q and HSAP by passive hemagglutination and by indirect immunofluorescence of HSAP-coated erythrocytes (E-HSAP). It is shown that although purified C1q binds HSAP, in the serum, the AAA and not C1q are responsible for the albumin binding activity in HBsAg-negative sera of patients with liver disease and of normal individuals, as detected by passive hemagglutination of E-HSAP, AAA were found to inhibit the binding of serum C1q to polymerized albumin, and hence the E-HSAP hemagglutination test for AAA titration in human sera proved valid.

Antibodies↗

PubMed1994

Transcapillary escape rate of albumin positively correlates with plasma albumin concentration in acute but not in chronic inflammatory disease.

The relationship among "negative" plasma acute-phase proteins (APP), ie, albumin, prealbumin, and transferrin, and "positive" APP, ie, C-reactive protein (CRP), fibrinogen, and orosomucoid, was investigated in patients with acute infectious disease (n = 8) and in patients with chronic malignant disease (n = 9). In addition, the transcapillary escape rate (TER) and outflux (J(alb)) of albumin were investigated using an intravenous injection of 2 microCi 125I-albumin. Interleukin-6 (IL-6) plasma concentrations were measured with an enzyme immunoassay. In the majority of patients, negative APP were decreased, whereas positive APP were increased. However, in patients with infectious disease, there were no significant correlations between any of the negative and positive APP. Also, in patients with infectious disease, TER was increased to 8.6 +/- 3.4%/h (mean +/- SD), and J(alb) to 114 +/- 60 mg/kg/h, compared with normal values of 4.3 +/- 2.6%/h and 108 +/- 7 mg/kg/h, respectively. Unexpectedly, there was a significant positive correlation between plasma albumin and both TER (r = .8279, P = .011) and J(alb) (r = .8683, P = .005). In patients with malignomas, significant correlations within negative and positive APP and inverse correlations between negative and positive APP resulted. Malignant disease induced only a slight elevation in TER (6.6 +/- 2.4%/h), J(alb) was within normal limits (92 +/- 35 mg/kg/h), and no correlations between plasma albumin concentrations and TER (r = -.0174, P = .97) or J(alb) (r = .4090, P = .27) were found.(ABSTRACT TRUNCATED AT 250 WORDS)

Acute Disease↗

PubMed1991

Structural characterization of a glycoprotein variant of human serum albumin: albumin Casebrook (494 Asp----Asn).

Albumin Casebrook is an electrophoretically slow genetic variant of human albumin with a relative molecular mass 2.5 kDa higher than normal albumin. It constitutes about 35% of total serum albumin in heterozygous carriers. The decrease in negative charge observed on incubation with sialidase suggested the presence of a carbohydrate moiety and the normalization of molecular weight following treatment with Endo-F indicated that this was an N-linked oligosaccharide. Partial acid hydrolysis and limited tryptic digestion established that the oligosaccharide was located in the C-terminal domain, between residues 367 and 585. Tryptic, chymotryptic and S. aureus V8 proteinase digestions were carried out and the resulting glycopeptides were purified on concanavalin A-Sepharose. Peptide mapping of bound and unbound fractions followed by amino acid composition and sequence analysis, established a point mutation of 494 Asp----Asn. This introduces an Asn-Glu-Thr N-linked oligosaccharide attachment sequence centered on Asn-494 and explains the increase in molecular mass. There was no apparent pathology associated with the presence of this new glycosylated albumin, which was detected in two unrelated individuals of Anglo-Saxon descent.

Amino Acid Sequence↗

PubMed2003

Behavior of various mammalian albumins towards bilirubin binding and photochemical properties of different bilirubin-albumin complexes.

Bilirubin (BR) binding properties of serum albumins from different mammalian species viz. human (HSA), equine (ESA), dog (DSA) and guinea pig (GPSA) were studied by absorption, fluorescence and CD spectroscopy. Whereas, a complex of BR with ESA produced maximum change, GPSA-BR complex showed weaker interaction as reflected from absorption and fluorescence spectroscopic data. Conformational analysis of these albumins by near- and far-UV CD spectra suggested similar structural characteristics (both secondary and tertiary structures) for ESA and HSA, whereas, DSA and GPSA had lower amounts of secondary and tertiary structures being minimum for GPSA. Photoirradiation results of BR-albumin complexes showed GPSA-bound BR more labile compared with other complexes, whereas, BR-ESA complex was found to be more stable against photoinduced chemical changes. Taken together, all these results suggest that chiroptical properties/stability of albumin bound BR varies with albumin species.

Albumins↗

PubMed1996

Observation of albumin resonances in proton nuclear magnetic resonance spectra of human blood plasma: N-terminal assignments aided by use of modified recombinant albumin.

Two-dimensional total shift correlation spectroscopy (TOCSY) and double-quantum-filtered phase-sensitive homonuclear shift-correlated spectroscopy (DQF-COSY) 1H NMR spectra are used to assign peaks for about one sixth of the amino acids residues of isolated human serum albumin (67 kDa) to amino acid types. Sequential assignments are presented for 1H NMR resonances of the N-terminal residues Asp1, Ala2 and His3 of human serum albumin (HSA). These are based on pH-dependent chemical shifts reflecting the titrating N-terminal NH2 and the His3 imidazole ring, in addition to DQF-COSY and TOCSY experiments. Studies of variant recombinant human albumin with Asp1 deleted, rHA(2-585), aided the assignments. The structural nature of the N-and C-termini of HSA are discussed and pKa values of 7.9 and 6.3 were determined for the N-terminal amino group and His3 imidazole ring, respectively. About 20 spin systems for albumin, including those for the N-terminal amino acids, were assigned in 1H NMR spectra of blood plasma buy comparison with isolated albumin. Resonances for lipids within lipoproteins and also several low molecular mass components can also be assigned in 2D TOCSY 1H NMR spectra of plasma.

Amino Acid Sequence↗

PubMed1978

The effect of dietary protein deficiency on albumin synthesis and on the concentration of active albumin messenger ribonucleic acid in rat liver.

In rats fed on a protein-deficient diet, albumin synthesis as a percentage of total liver protein synthesis falls from the normal value of approx. 15% to about 8%. We have extracted total cytoplasmic RNA from individual rat livers and measured the concentration of active albumin mRNA by translation in a reticulocyte lysate system from which the endogenous mRNA had been removed [Pelham & Jackson (1976) Eur. J. Biochem. 67, 247-256]. In this messenger-dependent system it is possible to measure the synthesis of albumin as a proportion of the overall protein synthesis promoted by the addition of the hepatic RNA. The results show that the concentration of translatable albumin mRNA in samples of total cytoplasmic RNA from livers of protein-deficient rats is decreased markedly. These findings suggest that dietary protein supply affects selectively the synthesis and/or functional stability of albumin mRNA in rat liver.

Albumins↗

PubMed1992

'Serum like' albumin of fowl seminal plasma and effects of albumin on fowl spermatozoa stored at 4 degrees C.

1. Using immunoelectrophoretic and immunodiffusion methods, serum-like albumin was detected in fowl seminal plasma. Immunodiffusion showed seminal plasma albumin concentration to be 4 mg/ml, corresponding to half of the total proteins (8 mg/ml). 2. Replacing seminal plasma with a diluent containing either 1, 4, or 16 mg/ml albumin increased motility of spermatozoa stored for 24 h at 4 degrees C, 16 mg/ml being the more effective dose. 1 and 4 mg/ml had no effect on the fertilising ability of fowl spermatozoa stored for 24 h at 4 degrees C in both young (28-35 weeks old) and old birds (50-55 weeks old). 16 mg/ml albumin had no effect on fertilising rates in young but depressed it in old birds. 3. These results indicate that seminal plasma albumin may be one of the mobility stimulating factors of seminal plasma. However it does not protect fertilising ability better than the diluent alone.

Albumins↗

PubMed2005

Are there advantages with U-Albumin/U-Creatinine ratios compared with U-Albumin in monitoring diabetes?

Management of hypertension and diabetes mellitus in primary health care requires occasional assessment of kidney function. Monitoring the urinary albumin excretion every 24 h is often used as a diagnostic gold standard but measurement of U-Albumin concentrations in morning urine either alone or together with U-Creatinine is a well-established surrogate measure. We compared the ratio U-Albumin/U-Creatinine and U-Albumin concentrations measured by commonly used POC (Point of care) instruments with those obtained in a central laboratory and estimated the uncertainty of the results after establishing an uncertainty budget. It is concluded that the presentation of ratios or concentrations on an ordinal scale is less satisfactory than reporting U-Albumin concentration on a ratio scale. Moreover the latter will have the advantage of allowing the physician to adjust the diagnostic sensitivity and specificity to local needs. The present report is a methodological study and does not consider the diagnostic performance of the studied properties per se.

Albumins↗

PubMed1980

The molar combining ratio of anti-albumin Fab' fragments to homologous and heterologous serum albumins.

The number of antibody combining sites on bovine (BSA), goat (GSA) and sheep (SSA) serum albumins was studied using rabbit and chicken antibodies. In homologous reactions, the profiles of quantitative precipitations with chicken antibody were similar to those with rabbit antibody reported previously (12), and the antigenic valence in the extreme antibody excess zone was found to be 6-7 for each albumin. The univalent Fab' fragments of rabbit and chicken antibodies were prepared. The stoichiometry of the soluble complex formed with the Fab' fragment and fluorescence labeled albumin was analyzed by gel filtration, and the number of Fab' fragment molecules capable of binding to an albumin molecule was estimated. In a homologous reaction with both rabbit and chicken Fab' fragments, the Fab' to albumin combining ratio revealed from the molecular weight of the soluble complex was 14:1. In the heterologous reactions, the combining ratio was 5:1 for rabbit Fab' fragments to BSA, and 9:1 for chicken Fab' fragment to BSA. From the heterologous reactions between GSA and SSA, it was demonstrated that the combining ratios were 10-11:1 with rabbit Fab' fragment and 11-13:1 with chicken Fab' fragment.

Antibodies, Anti-Idiotypic↗

PubMed1975

Binding of pyridoxal 5'-phosphate to bovine serum albumin and albumin fragments obtained after proteolytic hydrolysis. Localization and nature of the primary PLP binding site.

The binding of pyridoxal 5'-phosphate (PLP) to bovine serum albumin (BSA), and to large BSA fragments obtained after proteolytic hydrolysis, was investigated in order to study the structure of these fragments in relation to the albumin structure itself, and to get information about the PLP binding sites on albumin. From absorbance and circular dichroism spectra, combined with peptide mapping of the tryptic digests of the reduced PLP-protein complexes, it could be concluded that the primary binding site is localized with the NH2-terminal part of the albumin molecule. The COOH-terminal part contains one or more secondary sites. It appeared that in albumin and in the largest NH2-terminal fragment, the environment of the primary binding site is rather apolar in character. However, in the smallest NH2-terminal fragment this site is more exposed to the solvent. This suggests that the part of the peptide chain which is not common in both fragments has a stabilizing effect on the structure around the primary binding site.

Binding Sites↗

PubMed1993

Albumin modulation of paracellular permeability of pig vena caval endothelium shows specificity for pig albumin.

We measured endothelial hydraulic conductivity (Lp,e) and endothelial electrical resistance (Re) of pig vena cava in pig serum albumin (PSA) and bovine serum albumin (BSA) to determine whether specificity for the autologous albumin found in dog vena cava is a general property of mammalian endothelium. Pigs were anesthetized with pentobarbital sodium for surgical removal of the thoracic inferior vena cava. A vessel segment was placed as a membrane separating two compartments in a chamber. Vessels kept in 30 mg/ml BSA had Lp,e values of 1.30 +/- 0.81 x 10(-7) cm.s-1.cmH2O-1 (n = 9) and Re values of 13.8 +/- 2.6 omega.cm2 (n = 3). Vessels kept in PSA had Lp,e values of 0.257 +/- 0.125 x 10(-7) cm.s-1.cmH2O-1 (n = 5) and Re values of 21 +/- 6.3 omega.cm2 (n = 4). The differences between Lp,e and Re in BSA and PSA were statistically significant (P < 0.05). In vessels kept in PSA, switching to BSA caused a doubling of Lp,e. Lower Lp,e and higher Re in PSA as compared with those in BSA suggest that specificity for the autologous albumin is a general phenomenon in mammalian endothelium and that albumin binding to specific sites is associated with its permeability effect.

Animals↗

PubMed1974

Removing substances from blood by affinity chromatography. I. Removing bilirubin and other albumin-bound substances from plasma and blood with albumin-conjugated agarose beads.

Substances such as bilirubin that bind tightly to plasma proteins cannot readily be removed from blood. We describe here the use of affinity chromatography as a new approach to the removal of proteinbound metabolites and toxins from blood. Agarose beads were coupled via cyanogen bromide to human serum albumin so as to contain 30-50 mg of albumin/g wet wt. Such beads, when exposed to plasma from a patient with congenital nonhemolytic jaundice labeled with [(14)C]-bilirubin, bound more than 150 mug bilirubin/g of beads. The binding was saturable, concentration-dependent, relatively independent of flow rate, and reversible by elution with plasma, albumin, or 50% (vol/vol) ethanol. The beads could be repeatedly reused without loss of efficiency after ethanol elution and long storage in the cold. Salicylate, cortisol, and taurocholate, which bind weakly to albumin, were retarded by the beads but eluted with neutral buffer. Thyroxine, taurolithocholate, chenodeoxycholate, and digitoxin bound tightly but were eluted with 50% ethanol. Digoxin did not bind at all. When whole blood was passed over agarose-albumin beads, bilirubin was removed, calcium and magnesium fell slightly, but red cells, white cells, platelets, clotting factors, and a variety of electrolytes and proteins were substantially unchanged. Agarose-albumin beads may be useful for removing protein-bound substances from the blood of patients with liver failure, intoxication with protein-bound drugs, or specific metabolic deficits. Furthermore, it may be possible to make useful adsorbents by attaching other proteins to agarose or other polymer beads.

Bilirubin↗

PubMed1981

Biochemical and biophysical behaviors of plasma albumin. II. Comparison of plasma albumin from normal subjects and nephrotic patients.

Biochemical and biophysical analyses were made to study the properties of serum albumin from nephrotic patients of two types, remissive stage and relapsed state, and the results were compared with those in normal subjects. Two different ion exchange columns were prepared to isolate and purify each albumin sample and the materials eluted through the two columns were identified. The nephrotic elution materials, especially in the state of relapse, were of some difference from those of normal subjects. alpha-Helix contents estimated by circular dichroism spectra were found to be closer to normal albumin in remissive state than in the state of relapse. The binding of fluorescent probe, 1-anilino-8-naphthalene sulfonate, to albumin was examined by calculating the binding parameter, the dissociation constant and number of binding sites. The binding parameters were closer to those of normal albumin in remissive stage than the state of relapse.

Adolescent↗

PubMed1976

Alcohol, amino acids, and albumin synthesis. II. Alcohol inhibition of albumin synthesis reversed by arginine and spermine.

The effects of alcohol and spermine on albumin synthesis and polysome aggregation were studied in the isolated perfused rabbit liver system. Fed or fasted males served as donors and the perfusate contained, singly or in combination, alcohol, 200 mg per 100 ml, spermine, 1 mM, and arginine, 10 mM. The results indicate that in the presence of alcohol, using a liver from a fed donor, albumin synthesis is depressed from 16 to 6 mg per 100 g of wet liver weight per hr and the bound polysome is disaggregated. Spermine partially reaggregates the bound polysome and a combination of spermine and arginine augments albumin synthesis to the control rate. When the donor is fasted, and alcohol is present in the perfusate, the addition of spermine results in aggregated bound and free polysome patterns, whereas the combination of arginine and spermine is necessary to restimulate albumin synthesis. The results indicate that spermine plays an important role in the integrity of the polysome system and that arginine and spermine appears synergistic in maintaining albumin synthesis.

Albumins↗

PubMed1989

Affinity isolation of albumin-binding proteins using nitrocellulose-bound albumin.

Albumin immobilized on a nitrocellulose membrane was used as an affinity matrix to purify albumin-binding proteins (ABP) from extracts of lung, heart, thymus, and isolated microvascular endothelial cells. Albumin was immobilized onto nitrocellulose either (i) directly (physically adsorbed), (ii) cross-linked by treatment with 0.25% glutaraldehyde, or (iii) covalently coupled to the matrix using NaIO4 and Na-borohydride. The affinity support was incubated with a membrane-enriched fraction (obtained from tissue homogenates) in the presence of protease inhibitors; specific binding of ABP occurred within 30 min of incubation. The adsorbed proteins were eluted with 0.5% sodium dodecyl sulfate (SDS) and analyzed by SDS-polyacrylamide gel electrophoresis and ligand blotting. Analysis of electrophoretic mobility of eluted proteins showed that they consisted exclusively of the two sets of polypeptides of 31 000 Da and 18 000 Da previously identified as ABP (N. Ghinea et al., J. Cell Biol. 107, 231-239 (1988]. As demonstrated by ligand blotting, the ABP purified on nitrocellulose-bound albumin maintain the ability to interact specifically with albumin. Preliminary experiments showed that the method employed may be of a broader use for the isolation of receptor proteins from tissue extracts by incubating the latter with the cognate ligand immobilized on nitrocellulose membranes.

Albumins↗

PubMed1979

[Determination of drug-albumin binding in buffered bovine serum albumin solutions applying a modified ultrafiltration process (author's transl)].

The construction of two ultrafiltration devices which, under application of high-pressure liquid chromatographic (HPLC) technique, allow the determination of unbound portions of drugs in albumin solutions is described. The usefulness of this method and its advantages compared with prevailing methods are demonstrated by means of determination of the unbound portion of carbamazepine, chlorpromazine, phenobarbital and phenprocoumon in buffered bovine serum albumin solutions (4%). The binding of each drug to albumin was characterised by determining the overall binding constant (K1), the apparent binding constant (k+), the free reaction energy (delta F0), the number of binding sites per albumin molecule (n), the rate of taking up of drug by albumin (V) and the unbound portions of the drug (alpha).

Animals↗

PubMed1992

Albumin Rugby Park: a truncated albumin variant caused by a G-->C splice-site mutation in intron 13.

Three members of a family were found to be heterozygous for a fast albumin variant (Albumin Rugby Park) that made up only 8% of total serum albumin. Isoelectric focussing indicated an increased negative charge on the C-terminal CNBr peptide and C-terminal sequence analysis of the native protein showed an aberrant sequence of -Ser-Phe. Sequence analysis of PCR-amplified DNA indicated a G-->C mutation at position 1 of the 13th intron and this was confirmed by restriction digestion. The replacement of the obligate GT sequence by CT at the exon/intron boundary prevents splicing of the 13th intron and translation continues for 21 nucleotides until a stop codon is reached. The new protein lacks the 14 amino acids coded for in the 14th exon (GKKLVAASQAALGH), but these are replaced by 7 new residues (LLQFSSF), giving a truncated albumin of 578 residues.

Albumins↗

PubMed1980

Localization of the amino acid substitution site in a new variant of human serum albumin, albumin Mexico-2.

Using an electrophoretic screening procedure, we have discovered that two species of human serum albumin Mexico occur that are indistinguishable by conventional electrophoretic methods. We suggest that these species be referred to as albumins Mexico-1 and Mexico-2. Isolation and determination of the partial sequence of the cyanogen bromide fragment of albumin Mexico-2 that differs from the corresponding fragment of the common albumin A revealed this variant to arise from at least a glycine/aspartic acid substitution at position 550. This region of the albumin molecule is involved in the binding of the fatty acid, palmitate.

Journal Article↗