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At least 19 recordsLinked to original sources
PubMed1985

The effects of bovine serum albumin, bovine uterine fluid, and heat-treated bovine serum on in vitro mouse embryo development.

Two-cell mouse embryos were cultured in Whitten's medium with one of three supplements: bovine serum albumin (WM + BSA), heat-treated bovine serum (WM + HTBS) or bovine uterine fluid (WM + BUF). Protein concentrations for cultures of WM + BSA were 50.2, 100.5, 251.2, 502.5, and 1005.0 mug/ml and for WM + HTBS were 70.4, 105.1, 269.0, 524.5 and 1193.9 mug/ml. Protein concentrations ranged from 56.9 to 739.1 mug/ml for 22 WM + BUF samples. Embryo development in all media was significantly correlated with the log total protein concentration. When compared to WM + BSA, development was not significantly inhibited or stimulated in any WM + BUF cultures or in WM with 70.4, 524.5 and 1193.9 mug/ml HTBS. Development was enhanced in WM with 105.1 and 269.0 mug/ml HTBS (P<0.05). The results suggest that at the protein concentrations used, culture media supplemented with BUF and BSA support similar mouse embryo development. Culture medium supplemented with HTBS supported embryo development more than medium with BSA. Uterine factors in the bovine capable of enhancing or inhibiting early embryo development were not detected.

Journal Article↗
PubMed2005

Electrohydrodynamic atomization of protein (bovine serum albumin).

Bovine serum albumin (BSA) was chosen as a model protein. Three solutions of different concentrations of 5, 20 and 50 mg/ml were prepared, characterised and subjected to electrohydrodynamic atomization (EHDA). The 5 and 20 mg/ml solutions were atomized successfully and mode selection (M-S) maps were drawn for both concentrations to find out regions of stable cone-jet mode atomizaton. Droplet relics of these two solutions were investigated by electron microscopy. Samples were investigated by UV spectroscopy and circular dichroism (CD) spectroscopy before and after electrohydrodynamic atomization. We conclude that, particularly at the higher concentration of protein, EHDA does not result in significant structural change of BSA, and therefore is a processing route that can be considered for encapsulating drugs in proteins.

Drug Compounding↗
PubMed1985

Effect of sulfhydryl-disulfide state on protein phosphorylation: phosphorylation of bovine serum albumin.

Bovine serum albumin (BSA) was phosphorylated by the catalytic subunit of cAMP-dependent protein kinase under general protein phosphorylation conditions. The optimal pH for this phosphorylation was 9.0. The K0.5 (the concentration required for 50% of maximal phosphorylation) for BSA at pH 7.5 was 15 microM. One mole of phosphate was incorporated per mole of BSA, and only one phosphopeptide fragment was obtained after extensive proteolysis with trypsin. BSA phosphorylation required dithiothreitol or GSH, but GSH was only one-fiftieth as effective as dithiothreitol. GSSG counteracted the effect of dithiothreitol and GSH. Phosphorylation increased in a time-dependent and dithiothreitol concentration-dependent manner when BSA was preincubated with dithiothreitol. The increase in the incorporation of 32P correlated with the appearance of up to six free sulfhydryl groups. The effect of dithiothreitol on BSA appeared reversible, since reoxidation of reduced BSA decreased its susceptibility to phosphorylation. These experiments showed that this in vitro phosphorylation is dependent on the sulfhydryl-disulfide state of BSA. The possible implications of the sulfhydryl-disulfide state of proteins in the regulation of phosphorylation are discussed.

Animals↗
PubMed1990

The binding of palmitoyl-CoA to bovine serum albumin.

Bovine serum albumin (BSA) is routinely utilized in vitro to prevent the adverse detergent effects of long-chain acyl-CoA esters (i.e., palmitoyl-CoA) in enzyme assays. Determination of substrate saturation kinetics in the presence of albumin would only be valid if the relationship between bound and free substrate concentrations was known. To elucidate the relationship between bound and free palmitoyl-CoA concentrations in the presence of BSA, several different techniques including equilibrium dialysis, equilibrium partitioning, fluorescence polarization and direct fluorescence enhancement were investigated. Direct fluorescence enhancement using a custom synthesized fluorescent probe, 16-(9-anthroyloxy)palmitoyl-CoA (AP-CoA), was the best approach to this question. Measurement of the relationship between mol of palmitoyl-CoA bound per mol of BSA (nu) versus -log[free palmitoyl-CoA] revealed that the binding of palmitoyl-CoA to BSA, like palmitate was nonlinear, suggesting the presence of more than one class of acyl-CoA binding sites. Computer analyses of the binding data gave a best fit to the 2,4 two-class Scatchard model, suggesting the presence of two high-affinity primary binding sites (k1 = (1.55 +/- 0.46) x 10(-6) M-1) and four lower affinity secondary binding sites (k2 = (1.90 +/- 0.09) x 10(-8) M-1). Further analyses using the six parameter stoichiometric (stepwise) ligand binding model supports the existence of six binding sites with the higher affinities associated with the binding of the first mole of palmitoyl-CoA and weaker binding occurring after the first two sites are occupied. The association constants from this model of multiple binding diminish sequentially (i.e., K1 greater than K2 greater than K3 greater than...greater than or equal to K6), suggesting that each mol of long-chain acyl-CoA binds to BSA with decreasing affinities.

Acyl Coenzyme A↗
PubMed1982

Prolidase contamination in commercial bovine serum albumin.

Bovine serum albumin from a number of commercial sources were screened for the presence or absence of peptidase contamination. Peptidase activity was monitored using various peptides as substrates. Two commercial preparations were found to have peptidase activity, and the enzyme was identified, on the basis of its substrate specificity, as prolidase (EC 3.4.14.9). The contaminating activity was in the order of 3-4 units/g albumin.

Animals↗
PubMed1997

In-situ photochemical spectrofluorimetric detection of 9,10-anthraquinone-labeled bovine serum albumin.

Bovine serum albumin (BSA) labeled with 9,10-anthraquinone (AQ) shows a greatly enhanced photochemical fluorimetric activity compared with that of free AQ. The spectral characteristics of the photoreduction product of conjugated AQ were investigated and large blue shifts in the excitation and emission bands compared with those of free AQ were observed. The enhancement in the photochemical reactivity can be employed for sensitive detection of labeled BSA by a simple in-situ photochemical kinetic fluorimetric method. The kinetic behavior of the photochemical reaction and the effects of some experimental conditions were investigated. The calibration graph was linear over the range 0-1.8 x 10(-7) M BSA. The detection limit was 1.2 x 10(-10) M BSA and the relative standard deviation was 2.24% for 1.42 x 10(-8) M BSA (n = 7).

Anthraquinones↗
PubMed1997

In-situ photochemical spectrofluorimetric detection of 9,10-anthraquinone-labeled bovine serum albumin.

Bovine serum albumin (BSA) labeled with 9,10-anthraquinone (AQ) shows a greatly enhanced photochemical fluorometric activity compared with that of free AQ. The spectral characteristics of the photoreduction product of conjugated AQ was investigated and large blue shifts in the excitation and emission bands compared with those of free AQ were observed. The enhancement in the photochemical reactivity can be employed for sensitive detection of labeled BSA by a simple in-situ photochemical kinetic fluorimetric method. The kinetic behavior of the photochemical reaction and the effects of some experimental conditions were investigated. The calibration graph was linear over the range 0-1.8 x 10(-7) M BSA. The detection limit was 1.2 x 10(-10) M BSA and the relative standard deviation was 2.24% for the 1.42 x 10(-8) M BSA (n = 7).

Anthraquinones↗
PubMed1985

The delayed and saline wattle reactions in broilers challenged with bovine serum albumin.

Bovine serum albumin was used to study the development of a wattle reaction in broiler-type chickens. A strong response developed in both nonsensitized and sensitized chickens and the frequency of such was shown to be dependent on the method used for the sensitization. A similar swelling developed in a proportion of the wattles injected with saline and this too seemed to be influenced by the sensitization method. Moreover, both types of responses were shown to be somewhat unstable during the first 24 hr postchallenge.

Animals↗
PubMed1980

Inhibition of soluble guanylate cyclase by bovine serum albumin.

Bovine serum albumin (BSA) and to a lesser extent beta-lactoglobulin produced concentration-dependent inhibition of the guanylate cyclase activity in supernatant fraction and partially purified enzyme (PPE) prepared from rat lung homogenates. Ovalbumin had little effect. Some activity was lost when PPE was applied to a BSA-agarose column, however the loss disappeared when the enzyme reaction mixture contained Lubrol PX. Also, BSA no longer inhibited PPE after BSA-agarose treatment. BSA inhibition of PPE was not apparent when activity was maximally stimulated by arachidonate. These data were interpreted as indicating that the enzyme had bound to it an amphiphilic activator, possibly a fatty acid, the removal of which by BSA decreased activity.

Animals↗
PubMed1991

Culture of ovine embryos in the absence of bovine serum albumin.

Bovine serum albumin (BSA), a relatively impure protein, is routinely used as a component of embryo culture media. Since media containing BSA are chemically undefined, it would be desirable to replace BSA with substitutes of similar activity which are either chemically better defined and/or better standardized than BSA. Two commercial products, Ultroser((R)) G (USG) and Solcoseryl((R)) (SOL), were evaluated as replacements for BSA in culture with respect to the development of ovine embryos in vitro. A total of 126 late 8-cell and early 16-cell embryos were distributed among modified Brinster's medium for ovum culture (BMOC-2) containing either 1.5% BSA, 2.0% USG or 2.0% SOL. All three culture media supported development of ovine embryos. Results indicate that 8- and 16-cell embryos will develop into blastocysts in a BSA-free medium containing either USG or SOL. A higher number of embryos developed into blastocysts in media containing BSA than in media containing USG or SOL, and more blastocysts hatched in media containing BSA. Although the overall degree of embryonic development was more advanced in BSA-supplemented media, the concentrations of USG and SOL that were used in this study may not have been optimal for ovine embryo culture.

Journal Article↗
PubMed2001

The subsequent effect of interaction between Co(2+) and human serum albumin or bovine serum albumin.

A notable hysteretic effect has been observed in the interaction of Co(II) with human serum albumin (HSA) or bovine serum albumin (BSA) using UV-Visible spectrometry at physiological pH (7.43), which shows that the binding between Co(II) and HSA or BSA may induce a slow transition of HSA or BSA from the conformation of weaker affinity for Co(II) to one of stronger affinity (A-B transition). The rate constants and activation parameters of this transition were measured and are discussed. It is inferred that such a conformation transition may occur due to the binding of the first Co(II) ion with the peptide segment of N-terminal residues 1-3, which results in a 'hinged movement' of the relatively hydrophobic 'valley' in the IA subdomain. This process leads to a slow conformational transition in the albumins, makes the other binding sites of Co(II) exposed, and shows a positive cooperativity effect. The LMCT (ligand-to-metal charge transition) bands of the Co(II)-HSA and Co(II)-BSA systems also show a kind of hypochromic effect featuring a dipole-dipole interaction mechanism. This phenomenon is rarely reported.

Animals↗
PubMed2001

Monitoring for adsorption of human serum albumin and bovine serum albumin onto bare and polystyrene-modified silver electrodes by quartz crystal impedance analysis.

The adsorption of human serum albumin (HSA) and bovine serum albumin (BSA) from PBS (pH 7.4) onto bare and polystyrene (PS)-modified silver electrodes was in situ monitored using quartz crystal impedance analysis. The adsorption characteristics of HSA and BSA were discussed by analyzing piezoelectric parameter simultaneous responses. Experimental results indicated that for both HSA and BSA, the amount adsorbed on bare silver was more than that on PS-modified surface. The BSA amount adsorbed on the two surfaces was more than that of adsorbed HSA. A kinetic model was developed to describe the adsorption process and fitted to the experimental data of frequency shift. It was shown that HSA adsorption could be described by a kinetic equation involving two consecutive reactions. At lower concentration, BSA adsorption only involved the first reaction. At higher concentration, BSA adsorption on PS-modified surface involved two consecutive reactions. All fitted results were well in agreement with the corresponding experimental results. The regression values of reaction rate constants for the HSA and BSA adsorption were obtained. These data exhibited difference in adsorption kinetics under different conditions.

Adsorption↗
PubMed2006

Chiral resolution of tryptophan derivatives by CE using canine serum albumin and bovine serum albumin as chiral selectors.

This work deals with the application of BSA and canine serum albumin (CSA) for enantioseparation of tryptophan derivatives with CE. The aim of this work was the investigation of the influence of different functional groups of tryptophan derivatives on enantioseparation. CSA as a chiral selector was tested to compare its selector properties with those of BSA. The enantiomers of the tryptophan derivatives were separated by adding BSA or CSA to the BGE. The influence of pH, temperature, BSA and CSA concentration and organic modifiers was investigated. It was found that the stereoselectivity for the different tryptophan derivatives is dependent on the albumin species. It turned out that the different functional groups of the derivatives showed a significant influence on stereoselectivity.

Animals↗
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↗
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↗