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At least 19 recordsLinked to original sources
PubMed1978

Bovine serum albumin chronic serum sickness nephropathy in rats.

We administered bovine serum albumin (BSA) 1 or 3 mg i.v. into hyper-immune Sprague-Dawley rats weekly for up to 6 months. Animals with free circulating antibody 1 h after BSA developed mesangial deposits of IgG and C-3 without proteinuria. Rats without free antibody at 1 h developed either mesangial or mesangial and glomerular basement membrane (GBM) deposits. Rats given 3 mg BSA tended to have GBM deposits, proteinuria and undetectable antibody at 1 h. By electronmicroscopy, all rats had mesangial and subendothelial dense deposits, while those with GBM lesions had intramembranous and subepithelial deposits with foot process obliteration. Light microscopic evaluation of kidney tissue revealed only mild histological changes similar to those in age-matched control rats. The present studies demonstrate that prolonged i.v. administration of BSA into rats results in the development of a chronic non-inflammatory nephropathy. Despite certain parallels to chronic serum sickness nephropathy in rabbits, species differences appear to modify the nephropathy in rats.

Animals↗
PubMed1977

Serum amyloid A (SAA) protein-interaction with itself and serum albumin.

Serum amyloid A (SAA) protein is a 12,000 dalton protein that exists in serum under physiologic conditions as an 85,000 dalton complex and under certain conditions, as a 170,000 dalton component. To study the reason for this finding, the behavior of 125I-SAA was studied in the presence of cold SAA and several serum proteins. SAA caused a shift of some of the radioactivity to the region of albumin. Addition of normal human serum or albumin caused a shift of a significant fraction of the radioactivity to a peak eluting slightly ahead of albumin (80.000 daltons). This interaction could be blocked by the addition of cold SAA. No shift was noted when IgG or Bence Jones proteins were added. Thus, it appears that low molecular SAA protein has a tendency to aggregate with itself and to bind to albumin but not to human IgG or Bence Jones proteins.

Amyloid↗
PubMed1975

Brdicka currents observed with bovine serum albumin and completely reduced bovine serum albumin in the presence of urea.

In ammonia buffers of varying composition and pH, native bovine serum albumin and completely reduced bovine serum albumin, denoted by p(SH)35, yield quite different Brdicka current-voltage (i-E) curves, but they are identical in the presence of 5 mM calcium chloride. This means that in the presence of calcium, bovine serum albumin becomes completely reduced to p(SH)35. In 8 M urea and ammonia buffers the Brdicka i-E patterns of serum albumin and p(SH)35 are identical even in the absence of calcium, the effect of calcium on the first wave being negligible while calcium slightly increases the second wave. The maximum polarographic effect is attained at urea concentrations of about 5-6 M. Quite generally, the appearance of a second Brdicka wave is attributed to complexation of Co(II) with S- and a group of ligands that is different on the second than on the first wave. The effect of calcium on Brdicka currents of bovine serum albumin in the absence of urea is attributed to an orientation of the protein on the surface of the electrode such that all disulfide groups are reduced and with other ligands can complex with Co(ii). Denaturation of bovine serum albumin in buffers with a pH less than 10.5, and which are 8 M in area, is (polarographically) completely reversible if dilution is made within 15 minutes after preparation. Changes in Brdlcka I-E patterns upon longer aging at varying pH are attributed-in part at least-to dimerization of the denatured protein by interaction of pS- in one molecule with -S-S-in another.

Ammonia↗
PubMed1979

Delayed type hypersensitivity to bovine serum albumin and to lipid-conjugated bovine serum albumin in mice.

Delayed type hypersensitivity (DTH) to bovine serum albumin (BSA) and to lipid-conjugated BSA were studied comparatively. Unlike the case of BSA with which no DTH can be detected with native antigen, injection of butyric-conjugated BSA (Bu-BSA) in sensitized mice provokes a typical DTH for an early and limited period. Alum-precipitated Bu-BSA (Al-Bu-BSA) provokes from the beginning a stronger DTH which persists a much longer period.

Alum Compounds↗
PubMed1979

Immunochemistry of serum albumin. VI. A dynamic approach to the immunochemical cross reactions of proteins using serum albumins from various species as models.

Antisera against bovine serum albumin were raised in two rabbits. Serial bleedings were obtained at different times after the first immunization, and antisera from these serial bleedings were not mixed but were kept and studied separately. The immunochemical cross-reactions of these antisera with serum albumins from bovine, goat, sheep, porcine, horse, human and chicken were determined by immunoadsorbent studies. These were done by titration so that the values of maximum (plateau) binding by each albumin of radioiodinated antibodies were determined. In each rabbit, the immunochemical cross-reactivity was not static but increased progressievly with time after the first immunization. In the interval 7 days to 398 days the increases in cross-reaction were extremely large. pH dissociation studies revealed that, together with the increase in cross-reactivity of a given albumin with time after immunization, there was a restriction in the antibody heterogeneity towards populations possessing higher affinity. These results provide a rational explanation for the different values of cross-reactivities for a given albumin from different laboratories. The findings are analyzed in relation to the antigenic structure of albumin and their significance in evolutionary studies discussed.

Animals↗
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↗
PubMed1979

Fever induced in rabbits by intravenous injection of bovine serum albumin.

1. Bovine serum albumin injected into conscious rabbits produced a dose-dependent fever of short latency and duration of at least 2 1/2 hr. 2. The fever was not due to contamination by other proteins nor due to contamination by bacterial endotoxin. 3. The fever following albumin injection had characteristics similar to endogenous pyrogen fever. 4. Some traditional ways of distinguishing bacterial endotoxin fever from other types of fever need to be reassessed.

Animals↗
PubMed1978

Enhancement of the viscosity of mucin by serum albumin.

The interaction of serum albumin with a model epithelial mucin from pig stomach was explored by rotary viscometry. During 30 min of incubation of human serum albumin(20mg/ml) and pig gastric mucin (8mg/ml) in iso-osmotic buffers at 37 degrees C, the solution became markedly viscous. Viscosity enhancement was proportional to albumin concentration (2-40mg/ml), was most pronounced under conditions of low shear rate (less than 45S-1), and was considerably greater than the additive or multiplicative viscosity values calculated from albumin or mucin solutions measured separately. The viscous mucin-albumin complex was destroyed by high shear rates (greater than 90S-1), but slowly re-formed under zero shear conditions. Elevation of pH (7 to 9), ionic strength (0.1 to 1.0), and addition of disodium EDTA (5mM) did not cause marked or specific alterations in the viscosity of the mixture, suggesting that electrostatic interactions probably do not stabilize mucin-albumin complexes. Urea (7M) and heating (35 to 55 degrees C) caused a major increase in the viscosity of mucin and mucin-albumin mixtures, suggesting that rupture of hydrogen bonds, unfolding and partial denaturation of mucin promotes greater intertangling (possibly hydrophobic interactions) between mucin and albumin molecules. The implications of mucin-albumin interaction in diseases associated with mucus obstruction are briefly discussed.

Animals↗
PubMed1979

Bromocresol purple, a non-specific colour reagent for the determination of serum albumin.

The determination of serum albumin with the dye reagent bromocresol purple was investigated. We found that bromocresol purple is not a specific reagent for albumin, but that serum proteins in the alpha-, beta-, and gamma-globulin fractions also react with this dye. Similar results were obtained for bromocresol green. Furthermore there is a great difference in absorbance between human and bovine albumin solutions (having the same concentration) when using the bromocresol purple reagent. Most probably this is a result of the difference in interaction of the reagent with the substrate. Although the standard curves with the bromocresol purple method were more linear (especially at higher albumin concentrations) than those obtained with the bromocresol green method, we still prefer the bromocresol green technique to the bromocresol purple technique, because its results are more comparable with those of other methods. Moreover in quality control and calibration procedures, strong deviations from the recommended values are obtained when non-human sera are analyzed with the bromocresol purple method. For reasons of accuracy more specific methods are preferable.

Bromcresol Purple↗
PubMed1978

Binding of the organophosphates parathion and paraoxon to bovine and human serum albumin.

Binding of parathion and paraoxon to bovine serum albumin (BSA) and human serum albumin (HSA) was studied by using equilibrium dialysis. The concentration of unbound organophosphate was determined from its anticholinesterase activity. Binding of parathion to BSA was shown to be reversible. The organophosphates interact with only one type of binding sites in BSA and HSA. The affinity constants at pH 7.2 and 4 degrees C for the interaction of BSA or HSA and parathion were found to be 2.7 X 10(6) and 1.5 X 10(6) M-1, respectively. The affinity constants for the interaction of the serum albumins and paraoxon were considerably lower, 6.0 X 10(3) and 1.6 X 10(4) M-1, respectively. Lowering the pH from 7.2 to 4.8 did not significantly affect the binding parameters. The great difference of affinity of the serum albumins to parathion and paraoxon is discussed with respect to the fate of parathion in the body.

Animals↗
PubMed1977

Purification of intracellular forms of Plasmodium chabaudi and their interactions with the erythrocyte membrane and with serum albumin.

A procedure using bovine serum albumin gradients was developed for the separation of P. chabaudi-infected mouse erythrocytes from uninfected cells. This procedure can be used for the purification of erythrocytes containing different developmental stages of the parasite. The purified parasites were able to synthesize in vitro all the proteins that they are capable of synthesizing in vivo. The intracellular forms of P. chabaudi were found to be associated with erythrocyte membrane components and this associated membrane was shown to lack glycophorin. The free parasites bound albumin from serum; this binding, which showed some specificity with respect to the origin of the albumin, might play a role in the stabilization or protection of the extracellular parasites.

Animals↗
PubMed1976

Spectroscopic studies on the complex formation of suramin with bovine and human serum albumin.

The binding of suramin to bovine and human serum albumin was investigated by gel filtration and spectroscopic measurements. Besides some low-affinity binding sites suramin has, on the bovine serum albumin molecule one and on the human serum albumin molecule two, high-affinity binding sites. Spectroscopic measurements reveal that there are large differences between the albumins in the mechanism of binding to the high-affinity binding sites. Further, it is suggested that high concentrations of suramin provoke an unfolding of the albumin moleculse. In order to explain the unusual behaviour of suramin in connection with the displacement of other ligands from the albumin binding the fluorescence probe 1-anilino-8-naphthalenesulfonic acid (ANS) was employed as a reporter group molecule for fluorescence as well as circular dichroism measurements. By these measurements it could be shown that suramin greatly influences the microorganization of both albumin molecules. In the case of these measurements large differences between bovine and human serum albumin were also found.

Anilino Naphthalenesulfonates↗
PubMed1977

[Pigment Formation by Trichophyton rubrum: Differentiation between T. rubrum and T. mentagrophytes on Serum Albumin Agar (author's transl)].

On serum albumin agar (bovine albumin) with initial pH-values of 5.0-6.0, Trichophyton rubrum showed a yellow pigmentation, and on the same medium with an initial pH-value of 7.0, a red pigmentation. Strains of Trichophyton mentagrophytes have never shown pigmentation until now, The scarce growth (submerged) of T. rubrum on serum albumin agar is associated with a pigment formation that may be used for diagnostic purposes. It could be read within 3-7 days. Serum albumin agar with the initial pH-value of 5.0 was introduced in 1964 for the detection of the strain-specific proteolytic activity of Candida albicans.

Agar↗