BOVINE SERUM

Prepare competitor protein buffer detergent solution 4 mg/mL normal goat globulin or other competitor protein, (such as fetal calf serum, bovine serum albumin, bovine plasma, and so forth), and 0.1% saponin (Sigma, St. Louis, MO) in phosphate-buffered saline (NGG-sap-PBS). 

The deposition of the specific Ab on sNPS increases the photoluminescence level, but upon formation of the specific immune complex it decreases. The level of photoluminescence decrease depends on the concentration of T2 mycotoxin in the solution (Fig. 9.8). If a non-specific antibody is used or serum bovine albumin is used as an antigen the photoluminescence level does not change. 

Neurological Effects. Little information was available to determine the neurotoxicity or the mechanism of neurotoxicity of HDI after inhalation, oral, or dermal exposure. Headache was reported in only one human exposure case (Malo et al. 1983). Neurotoxic effects (convulsions) may occur in laboratory animals if concentrations reaeh high levels in the air (Haskell Laboratory 1961) however, sinee HDI is metabolized quickly in a biological matrix (Berode et al. 1991), little intaet HDI is expected to reach the nervous tissue to elicit a toxic response, except possibly at very high eoneentrations. No neurological effects have reported in laboratory animals, or in hiunans exposed chronieally to low concentrations of HDI (Mobay Corporation 1989). HDI, in addition to other isocyanates, have been shown to inhibit acetylcholinesterase in human erythrocytes (Dewair et al. 1983), human serum acetylcholinesterase (Brown et al. 1982), as well as equine serum, bovine erythrocyte, and eel acetylcholinesterase (Brown et al. 1982). 

Serum, bovine liver (total) Digestion of sample with HNOs and heat in closed container in microwave oven reduction with SnCI2 and TBP purging to gold-coated sand adsorber to preconcentrate (amalgamation) thermally desorb to detector CVAAS 0.84 ng/g 93-111 Vermeiret al. 1989... 

Hanke, D.W. and Overton, M.A. 1991, Phosphylation kinetic constants and oxime-induced reactivation in acetylcholinesterase from fetal bovine serum, bovine caudate nucleus, and electric eel, J. Toxicol Environ. Health, vol. 34, no. 1, pp. 141-156. 

Using new and very clean equipment, you should inject at least 4—5 times a standard sample mixture to saturate the hungry surfaces use for protein SB A (serum bovine albumin). 

Milk, pork and lat liver, pork serum, bovine mammary gland, pork sub-nuudllary gland, calf thyroid, goat colostrum, and other tissues... 

Albumins are a family of globular proteins, the most common of which is serum albumin. The albumin family consists of aU proteins that are water-soluble, are moderately soluble in concentrated salt solutions, and experience heat denatura-tion. Albumins are commonly found in blood plasma they are unique from other blood proteins in that they are not glycosylated. Substances containing albumins, such as egg white, are called albuminoids. Commercially, albumins are obtained insignificant quantities from egg white (ovalbumin), bovine serum (bovine serum albumin, BSA), and human serum (human serum albumin, HSA). They are also available from soybeans, milk, and grains [101-103]. 

Kurrat R, Prenosil J E and Ramsden J J 1997 Kinetios of human and bovine serum albumin adsorption at silioa-titania surfaoes J. Colloid Interface Sol. 185 1-8... 

This experiment provides a nice example of the application of spectroscopy to biochemistry. After presenting the basic theory for the spectroscopic treatment of protein-ligand interactions, a procedure for characterizing the binding of methyl orange to bovine serum albumin is described. 

This experiment describes the adaptation of the bicinchoninic acid (BCA) protein assay to a flow injection analysis. The assay is based on the reduction of Cu + to Cu+ by the protein, followed by the reaction of Cu+ with bicinchoninic acid to form a purple complex that absorbs at 562 nm. Directions are provided for the analysis of bovine serum albumin and rabbit immunoglobulin G, and suggestions are provided for additional analyses. 

The bovine serum albumin molecule is known to be nearly spherical and uncharged in a solution of pH 5.37. A plot of n/c2 versus C2 for this polymer at 25°C is linear and has an intercept corresponding to M = 69,000. The slope of the line is 1.37 X 10" Torr liter g . Use this slope to estimate the radius of this spherical molecule. 

Compare the two methods in terms of the assumptions involved, the supple mentary information required, and the sensitivity to experimental error 11. The following values of n/c2 versus C2 were measuredf at 25°C in 0.15 NaCl solutions for bovine serum albumin ... 

A hybridoma can live indefinitely in a growth medium that includes salts, glucose, glutamine, certain amino acids, and bovine serum that provides essential components that have not been identified. Serum is expensive, and its cost largely determines the economic feasibihty of a particular ciilture system. Only recently have substitutes or partial replacements for serum been found. Antibiotics are often included to prevent infection of the culture. The pH, temperature and dissolved oxygen, and carbon dioxide concentration must be closely controlled. The salt determines the osmotic pressure to preserve the integrity of the fragile cell. 

Human serum albumin has been purified similarly with 25% EtOH and 0.2% decanol. The isoelectric points of bovine and human serum albumins are 5.1 and 4.9. 

Transferrin (from human or bovine serum) [11096-37-0] Mr 80,000. Purified by affinity... 

A second method uses sodium periodate (NaI04) as the oxidant in the presence of the readily available protein bovine serum albumin. In this procedure, the sulfide is complexed in the chiral envirorunent of the protein. Although the oxidant is achiral, it encounters the sulfide in a chiral envirorunent in which the two faces of the sulfide are differentiated. 

The effect of flow rate on resolution by Toyopearl HW-55F and Toyopearl HW-55S columns has been studied using a bovine serum albumin sample. Eor both columns, resolution decreased with increasing flow rate (46). Resolution is increased, however, with decreasing particle size (47). Resolution is proportional to the square root of the column length, as theoretically expected, and indicates that longer columns can be packed as well as shorter columns. Therefore, for samples difficult to resolve, the solution may be to increase the column length. 

Three different types of columns packed with gels of different pore sizes are available. Columns should be selected that are suitable for the molecular weight range of specific samples, as each type has a different exclusion limit (Fig. 6.41, page 215). Bovine serum albumin (BSA), myoglobin, and lysozyme show good peak shapes using only 100 mM of sodium phosphate buffer as an eluent. There is no need to add any salt to the eluent to reduce the ionic interaction between protein and gel. 

FIGURE 7.10 Dependence of the resolution on the sample volume. A preparative Superformance column 1000-200 (bed volume 20 liters) packed with Fractogel END BioSEC (S) (bed height 63 cm) was loaded with 60 ml (top) and 300 ml of a mixture of bovine serum albumin (5 mg/ml), ovalbumin (5 mg/ml), and cytochrome c (3 mg/ml) (bottom) (20 m/VI sodium phosphate buffer, 0.3 M NaCI, pH 7.2 flow rate 100 ml/min corresponding to 19 cm/hr). When the sample volume is 300 ml the separation efficiency for BSA and ovalbumin is similar. Thus the column can be loaded with larger sample volumes, resulting in reasonable separations. 

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