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At least 325 records · Page 18Linked to original sources
PubMed1986

Serum albumin and cyanide detoxication. Kinetic characterization of a reactive albumin-sulfur complex.

Kinetic studies of the serum albumin-catalyzed reaction of cyanide with colloidal elemental sulfur have been carried out to elucidate the formal mechanism of this reaction. The results indicate that one of the several sulfur-binding sites on the protein molecule is involved in a single displacement catalytic cycle in the presence of cyanide. At high velocities the rate of thiocyanate production is limited by an albumin-independent second order process which produces the form of sulfur that serves as substrate. The catalyzed reaction is also subject to substrate inhibition at high colloidal sulfur concentrations.

Cyanides↗
PubMedDate not supplied

Binding of sulfonylurea derivatives to bovine serum albumin: part II. The relationship of binding to albumin, chemical structure, and hypoglycemic activity of sulfonamide derivatives of 2-pyrazoline-1-carboxamide.

The relationship of binding to protein and hypoglycemic activity of 11 sulfonamide derivatives of 2-pyrazoline-1-carboxamide was tested. It has been shown that the hypoglycemic effect of the most potent compound of the series, SPC-703, is related to the unbound, but not to the total concentration of the drug in the rat serum. Binding to albumin increased with the increase of hydrophobic properties of the compounds investigated. The increased affinity to albumin may be responsible for low hypoglycemic activity of some of the compounds tested.

Animals↗
PubMed1981

The evolution of alpha-fetoprotein and albumin. I. A comparison of the primary amino acid sequences of mammalian alpha-fetoprotein and albumin.

The amino acid sequence of mouse alpha-fetoprotein has been deduced from the nucleotide sequence of its mRNA and three chimeric plasmids containing overlapping segments of its cDNA. A comparison of the amino acid sequence with that of either human and bovine albumin reveals in each case a 32% conservation of primary sequence. In addition, using the regularly spaced positions of cystine bridges, a 2-dimensional structure was generated, which revealed the presence of 3 closely related domains within alpha-fetoprotein. The structures of these domains are identical with the triplicated domains previously observed in several mammalian albumins. These homologies lend strong circumstantial evidence to the proposal that these two proteins arose in evolution as the consequence of a duplication in a common tripartite ancestral gene.

Albumins↗
PubMed1984

Glomerular albumin leakage and morphology after neutralization of polyanions. I. Albumin clearance and sieving coefficient in the isolated perfused rat kidney.

In order to decide whether foot process abnormalities in nephrotic states are the cause or the consequence of proteinuria, the polycation protamine has been applied to isolated perfused rat kidneys and functional parameters and morphology have been compared. With 110 micrograms/ml protamine the albumin clearance ratio increased from 2.0 +/- 0.7 x 10(-3) in controls to 14.8 +/- 6.9 x 10(-3) 10-20 min after application and even to 98.0 +/- 30.8 x 10(-3) after 50-80 min. Micropuncture samples collected from early proximal tubules with pressure control were used to calculate the sieving coefficient which correlated with albumin clearance ratios (controls: 1.8 +/- 1.0 x 10(-3); after 10-20 min: 11.8 +/- 6.4 x 10(-3); after 50-80 min: 52.0 +/- 8.5 x 10(-3). Glomerular filtration rate decreased in the early beginning from 1.1 +/- 0.2 ml x min-1 x g-1 kidney to 0.7 +/- 0.2 ml x min-1 x g-1 kidney, but remained constant throughout the whole experiment. Despite the markedly increased albuminuria there were no changes in glomerular foot process morphology with the protamine dose used.

Albumins↗
PubMedDate not supplied

[Comparative analysis of the effect of active immunization of rats with bovine serum albumin and serotonin-bovine serum albumin conjugate on brain biogenic amine levels and behavioral reactions].

The authors studied the effect of active immunization of rats with bovine serum albumin and serotonin-bovine serum albumin conjugate on the distribution of biogenic amines in the brain and the behaviour of the animals. It is shown that the effect of the studied antigens on the condition of the brain mediator systems and the animals' behaviour differ in their trend, which must be taken into account in choosing adequate control in studies with induction of antibodies against low-molecular substances by means of conjugated antigens.

Animals↗
PubMed1976

A study performed on batches of serum albumin used as diluents in Rh testing. A report to the International Society of Blood Transfusion/International Committee for Standardization in Haematology by their albumin working party.

The paper reports the findings of a Working Party of the Joint International Committee of Standardization/International Society of Blood Transfusion on the Standardization of Blood Group Reagents. Thirteen samples of serum albumin, 11 bovine and two human, were examined by serological and physicochemical means. Batches of albumin tested were normally more efficient in causing agglutination of sensitized red cells than in aiding the uptake of Rh antibody, and those found satisfactory by manual techniques gave satisfactory results by automated methods. Reference is made to evidence for the existence of inhibitors of red cell agglutination which may account for lack of correlation noted between the dimer/polymer content of some samples and their efficiency in causing agglutination of sensitized red cells.

Animals↗
PubMed1985

Normal variations in rate of albumin excretion and albumin to creatinine ratios in overnight and daytime urine collections in non-diabetic children.

Urine albumin excretion measured over consecutive weekends and on repeated first morning collections from normal children showed considerable variation both during the day and from day to day in each subject. The results emphasise the need for repeated measurement of albumin excretion in children to confirm the presence of persistent microalbuminuria.

Adolescent↗
PubMed2002

Is albumin gradient or fluid to serum albumin ratio better than the pleural fluid lactate dehydroginase in the diagnostic of separation of pleural effusion?

BACKGROUND: To determine the accuracy of serum-effusion albumin gradient (SEAG) and pleural fluid to serum albumin ratio (ALBR) in the diagnostic separation of pleural effusion into transudate and exudate and to compare SEAG and ALBR with pleural fluid LDH (FLDH) the most widely used test. METHODS: Data collected from 200 consecutive patients with a known cause of pleural effusion in a United Kingdom district general hospital. RESULTS: The median and inter quartile ranges (IQR) for SEAG 93.5 (33.8 to 122.5) g/dl, ALBR 0.49 (0.42 to 0.62) and FLDH 98.5 IU/L(76.8 to 127.5) in transudates were significantly lower than the corresponding values for exudates 308.5 (171 to 692), 0.77 (0.63 to 0.85), 344 (216 to 695) all p < 0.0001. The Area Under the Curve (AUC) with 95% confidence intervals (Cl) for SEAG, ALBR and FLDH were 0.81 (0.75 to 0.87), 0.79 (0.72 to 0.86) and 0.9 (0.87 to 0.96) respectively. The positive likelihood ratios with 95%CI for FLDH, SEAG, and ALBR were: 7.3(3.5-17), 6.3(3-15) 6.2(3-14) respectively. There was a significant negative correlation between SEAG and ALBR (r= -0.89, p < 0.0001). CONCLUSION: The discriminative value for SEAG and ALBR appears to be similar in the diagnostic separation of transudates and exudates. FLDH is a superior test compared to SEAG and ALBR.

Journal Article↗
PubMed1981

On the standardisation of the direct spectrophotometric bilirubin determination. Influence of the albumin source and the molar bilirubin: albumin ratio.

The influence of different albumin solutions and of the molar bilirubin/albumin ratio on the bilirubin concentration determined by the method for Hertz et al. was studied. There is good agreement between the true-bilirubin concentrations and those obtained by the Hertz method for bilirubin-HSA and bilirubin-serum solutions. Moreover the observed concentration is scarcely influenced by the molar ratio. Bilirubin standards in HSA-solutions can thus be used to standardise this method. Errors are introduced by preparing standards in BSA-solutions as the absorption spectrum of bilirubin-BSA is different from that of bilirubin-HSA.

Bilirubin↗
PubMed1992

X-band electron paramagnetic resonance spectra of bovine serum albumin-copper(II) and bovine serum albumin-copper(II)-aminoacid systems.

X-band electron paramagnetic resonance (epr) spectra of the binary systems, BSA-copper(II) (1:1 and 2:1), and the ternary systems, BSA-Cu(II)-aminoacid (1:1:1), are described. In the binary system, two distinct epr features have been observed. One of the features (towards the low pH), showing broad and overlapping epr signals, has been attributed to non-specific bonding of copper(II) to the albumin and other feature (towards higher pH), showing sharp intense epr signals, has been attributed to the specific bonding. The change from non-specific to specific binding is favoured by increase in pH as well as by increase in protein concentration. Specific binding of copper(II) in BSA-Cu(II) has been suggested to be similar to that in HSA-Cu(II). Spectra of BSA-Cu(II)-aminoacid (1:1:1) show simultaneous presence of binary BSA-Cu(II) and ternary BSA-Cu(II)-aminoacid.

Amino Acids↗
PubMed1989

[The possibility of using equine serum albumin in place of bovine serum albumin and ovalbumin in radioimmunological and immunoenzyme analyses and in virological practice].

Horse serum albumin has been shown to meet the requirements to protein preparations for microanalysis and thus to be suitable for use in kits of reagents for the radioimmunological determination of insulin and myoglobin, for the determination of tick-borne encephalitis virus antigen by the method of the enzyme immunoassay and for the stabilization of proteins in the hemagglutination test and the hemagglutination inhibition test.

Animals↗
PubMed1996

Co-integration of beta-lactoglobulin/human serum albumin hybrid genes with the entire beta-lactoglobulin gene or the matrix attachment region element: repression of human serum albumin and beta-lactoglobulin expression in the mammary gland and dual regulation of the transgenes.

The effect of co-integration of the entire beta-lactoglobulin (BLG) gene or matrix attachment region (MAR) sequences on the expression of various BLG/ human serum albumin (HSA) gene constructs was tested in transgenic mice. These former sequences were chosen because of their reported ability to insulate transgenes from the neighboring host genomic DNA sequences and/or to provide a more permissive transcriptional environment. When introduced alone, a cDNA-based BLG/HSA construct was expressed in 60% of transgenic strains and HSA was secreted at levels up to 0.3 mg/ml into the milk. Upon co-integration with either the entire BLG gene or MAR element, HSA RNA and protein expression were completely abrogated. While the co-integrated BLG gene suppressed the proportion of expresser strains carrying cDNA as well as genomic BLG/HSA constructs, the MAR element only exerted its negative effect on the cDNA-based BLG/HSA construct. In transgenics expressing both HSA and BLG, the tissue specificity and developmental patterns of BLG expression were altered and resembled the less stringent pattern of the BLG/HSA expression. These results demonstrate that rescue of transgene expression through co-integration with BLG or MAR sequences do not apply universally.

Animals↗
PubMed1999

Interaction of human serum albumin with furosemide glucuronide: a role of albumin in isomerization, hydrolysis, reversible binding and irreversible binding of a 1-O-acyl glucuronide metabolite.

Furosemide 1-O-acyl glucuronide (Fgnd) was reversibly bound to a single class of binding sites on human serum albumin (HSA), and the binding of Fgnd decreased with increasing F concentrations, suggesting that Fgnd binds to the same warfarin binding sites on HSA as F binds. The rate of Fgnd degradation (hydrolysis and acyl migration) decreased in the presence of HSA. Although the formation of acyl migration isomers of Fgnd was slower in the presence of HSA than in its absence, hydrolysis of Fgnd to F was faster in the presence of HSA. Rapid minor irreversible binding of Fgnd to HSA within 30 min was followed by slow major irreversible binding. Slow irreversible binding of Fgnd to HSA was decreased by F, though not significantly. This suggests that major irreversible binding may proceed via reversible binding. It has been reported that acyl migration is a prerequisite for irreversible binding. Therefore, these results indicate that HSA decreases irreversible binding of Fgnd to protein by suppressing acyl migration. Furthermore, these results suggest that HSA may prevent irreversible binding of Fgnd to other proteins in the body by decreasing the concentration of reactive Fgnd in the unbound form. HSA eliminates reactive Fgnd by hydrolysis to F. Therefore, it is concluded that HSA works as a scavenger to decrease reactive compounds by reversible binding or eliminates reactive compounds by irreversible binding.

Acylation↗
PubMed1993

Influence of specific albumin ligand markers used as modifiers on the separation of benzodiazepine enantiomers by chiral liquid chromatography on a human serum albumin column.

Specific ligand markers for the various binding sites of human serum albumin (HSA) have been described in the literature. Some of these markers (medium chain fatty acids, warfarin, digoxin, and bilirubin) were used as mobile phase modifiers. Using a high performance liquid chromatographic (HPLC) column containing HSA as stationary phase, their influence was investigated on the separation in this phase of the enantiomers of three benzodiazepines (temazepam, oxazepam, and lorazepam). Displacement effects were observed with medium chain fatty acids. This influence was proportional to the chain length and to the concentration of acid. Allosteric cooperative effects were noted with digoxin for the three benzodiazepines. Both displacement and cooperative effects were observed with warfarin. Stereoselectivity was decreased for temazepam and oxazepam and increased for lorazepam.

Anti-Anxiety Agents↗
PubMed1987

Interactions between hepatitis B virus and polymeric human albumin. I. Production of monoclonal anti-idiotypes (anti-anti-polymeric human albumin) which recognize hepatitis B virus surface antigen.

In an attempt to characterize the polymeric human albumin (polyHSA) receptor expressed on hepatitis B virus and hepatocytes, we have used a human anti-polyHSA IgG to generate monoclonal anti-idiotypes (anti-Id) which bear the internal image of polyHSA and mimic its binding activity. Two monoclonal anti-Id antibodies, 63.14 and 70.F9, were strongly reactive in both radioimmunoassay and enzyme-linked immunosorbent assay (ELISA) with the F(ab')2 of the immunogen as well as with purified hepatitis B surface antigen (HBsAg) expressing various subtypes. The specificity of the binding of anti-Id to HBsAg was confirmed in direct ELISA and by Western blot analysis. These experiments also showed that the anti-Id bind to a site expressed on the major 24-kDa protein of HBsAg particles, and that this recognition is specifically inhibited by polyHSA. Experiments on cellular staining and radioimmunoprecipitation on HBsAg-positive and -negative cell lines showed that the anti-Id recognize intracellular HBsAg but not other liver cell proteins, including the putative polyHSA receptor. These data indicate, therefore, that the monoclonal anti-Id mimic the binding activity of polyHSA and recognize its binding site on the virus. The inability of both anti-Id to react with the hepatocyte surface suggests either the absence of a specific hepatic polyHSA receptor or the expression of one with a different configuration.

Antibodies, Monoclonal↗
PubMedDate not supplied

Presence of serum albumin in normal human epidermis: possible implications for the nutrition and physiology of stratified epithelia. Presence of albumin in epidermis.

In this paper, using both immunofluorescence and protein biochemistry techniques, we present definitive evidence that plasma proteins such as albumin are present within normal human epidermis. This result confirms several previous reports supporting the idea that relatively large molecules can diffuse through the epidermal basement membrane into epidermis. Our results bring new insights for discussing how hydrophobic ligands or drugs present in the bloodstream and bound to plasmatic carriers can reach epidermal cells of all layers.

Electrophoresis, Gel, Two-Dimensional↗
PubMed1990

Thyroxine binding to human serum albumin immobilized on sepharose and effects of nonprotein albumin-binding plasma constituents.

125I-thyroxine (125I-T4) binding to human serum albumin (HSA) covalently attached onto CNBr-activated Sepharose (HSA-Sepharose) was studied. 125I-T4 binding to HSA-Sepharose was rapid and saturable. Nonlinear curve-fitting analysis of binding isotherms revealed two classes of binding sites. The values of dissociation constants of high and low affinity sites were 2.19 +/- 0.53 x 10(-6) M and 2.69 +/- 0.78 x 10(-5) M, respectively. The number of binding sites of the high and the low affinity sites were 1.28 +/- 0.46 mol/mol and 23.5 +/- 9.7 mol/mol of HSA, respectively. Fatty acids and bilirubin competitively inhibited the high-affinity binding of 125I-T4 to HSA-Sepharose without affecting the low-affinity binding. 8-anilino-1-naphthalene sulfonic acid (ANS) inhibited the high affinity T4 binding via reduction of the binding capacity. Unlabeled T4 showed little inhibition of ANS binding to HSA, as measured by fluorescence intensity. These results suggest that ANS allosterically inhibits the high-affinity T4 binding to HSA-Sepharose.

Anilino Naphthalenesulfonates↗
PubMed1994

Specific combinations of human serum albumin introns direct high level expression of albumin in transfected COS cells and in the milk of transgenic mice.

A new series of expression vectors, each comprised of the beta-lactoglobulin (BLG) promoter driving one of a variety of human serum albumin (HSA) minigenes or the entire gene, were evaluated for their ability to direct expression of HSA in vitro in COS tissue culture cells and into the milk of transgenic mice. Vectors directed a hierarchy of expression levels in vitro, dependent upon the specific complement of HSA introns included. HSA introns acted in a synergistic manner. In addition, minigenes comprised of specific subsets of introns were more efficacious than the entire HSA gene with all of its introns. Transgenic mice expressed as much as 10 mg ml-1 of HSA in their milk. Vectors comprised of specific intron subsets directed levels at 1 mg ml-1 or greater in the milk of 20% of generated transgenics. A statistical correlation between the expression level trend in vitro with the trend of expression in vivo (% which express) at detectable levels (p = 0.0015) and at the level of greater than 0.1 mg ml-1 (p = 0.0156) was demonstrated. A weak correlation existed (p = 0.0526) at in vivo levels of 1 mg ml-1 or greater. These new vectors are expected to direct the production of high levels of HSA in the milk of a large percentage of generated transgenic dairy animals.

Animals↗