Chemicals bovine serum albumin

The urease is incorporated into a polyacrylamide gel which is allowed to set on the bulb of the glass electrode and may be held in position by nylon gauze. Preferably, the urease can be chemically immobilised on to bovine serum albumin or even on to nylon. When the electrode is inserted into a solution containing urea, ammonium ions are produced, diffuse through the gel and cause a response by the ammonium ion probe ... 

Protein concentration can be determined using a method introduced by Bradford,4 which utilises Pierce reagent 23200 (Piece Chemical Company, Rockford, IL, USA) in combination with an acidic Coomassie Brilliant Blue G-250 solution to absorb at 595 nm when the reagent binds to the protein. A 20 mg/1 bovine serum albumin (Piece Chemical Company, Rockford, IL, USA) solution will be used to prepare a standard calibration curve for determination of protein concentration. The sample for analysis of SCP is initially homogenised or vibrated in a sonic system to break down the cell walls. 

Shaw, C.F. Ill, Schaeffer, N.A., Elder, R.C., Eidsness, M.K., Trooster, J.M. and Calls, G.H.M. (1984) Bovine serum albumin-gold thiomalate complex gold-197 Moessbauer, EXAFS and XANES, electrophoresis, sulfur-35 radiotracer, and fluorescent probe competition studies. Journal of the American Chemical Society, 106, 3511-3521. 

Materials. Microspherical PGG glucan (Adjuvax, Alpha-Beta Technology, Worcester, MA) was prepared from Saccharomyces cereviseae strain R4 cells (11). Zymosan, cytochrome c (cyt c), bovine serum albumin (BSA), yeast alcohol dehydrogenase (ADH), Complete Freunds Adjuvant (CFA) and Incomplete Freunds Adjuvant (IFA) were purchased from Sigma Chemical Co. (St. Louis, MO). 

Mir MM, Fazili KM, Abul Qasim M. Chemical modification of buried lysine residues of bovine serum albumin and its influence on protein conformation and bilirubin binding. Biochim. Biophys. Acta 1992 1119 261-267. 

An alternative approach to the production of subunit vaccines entails their direct chemical synthesis. Peptides identical in sequence to short stretches of pathogen-derived polypeptide antigens can be easily and economically synthesized. The feasibility of this approach was first verified in the 1960s, when a hexapeptide purified from the enzymatic digest of tobacco mosaic virus was found to confer limited immunological protection against subsequent administration of the intact virus. (The hexapeptide hapten was initially coupled to bovine serum albumin, used as a carrier to ensure an immunological response.)... 

In this method the keyhole limpet haemoglobin conjugate was prepared as follows Keyhole limpet haemocyanin (KLH, Calbiochem, La Jolia, CA) and bovine serum albumin (BSA, BDH Chemicals) were coupled to the adduct (2), derived from 6-bromohexanoic acid and monoquat (3), via a carbodiimide reaction, as reported previously by Niewola et al. [184], The resulting conjugates contained 662mol of Paraquat per mole of KLH and 15mol of Paraquat per mole of 6-bromohexanoic acid. The amount of Paraquat bound to the protein was determined by spectrophotometric dithionite assay for Paraquat and the protein concentration was established by a standard Lowry test. 

Fig. 41. LS plots for solutions of bovine serum albumin (concentration c2) in aq. 6 M guanidine hydrochloride, obtained at constant molarity C3, constant chemical potential n3 and constant molality m3 of guanidine hydrochloride. The resultant molecular weights yielded for this sample are given above each plot15)...

X 10 2 M Tris HC1 buffer, pH 7.5, 2.4 X 10 3 M glucose 6-phosphate (G-6-P), 1.6 units glucose 6-phosphate dehydrogenase (G-6-P dH), 5.1 X 10"5 M NADP, and 2.7 X 10 3 M KC1. In addition, the following chemicals were included in the final concentration indicated 5.1 X 10-3 M NADH, 1% (W/V) bovine serum albumin (BSA), and 1.0 mg aldrin in 0.1 ml ethanol. Whole body homogenate experiments included all of the above chemicals unless otherwise noted. Reaction mixtures were incubated with swirling in test tubes at 30 - 1°C. Reactions in Steps 1-4 of the experimental sequence were stopped after 1 hr and Steps 6-8 after 15 min, by the addition of 2 ml 5% TCA. 

Chemical reactions Polymerization of casein and whey proteins are due to some kind of chemical reactions. The different proteins as found in the supernatant of milk after precipitation at pH 4.6 are collectively called whey proteins. These globular proteins are more water soluble than caseins and are subject to heat dena-turation. Denaturation increases their water-binding capacity. The principal fractions are P-lactoglobulin, a-lactalbumin, bovine serum albumin (BSA), and immunoglobulins (Ig). 

Urea in kidney dialysate can be determined by immobilizing urease (via silylation or with glutaraldehyde as binder) on commercially available acid-base cellulose pads the process has to be modified slightly in order not to alter the dye contained in the pads [57]. The stopped-flow technique assures the required sensitivity for the enzymatic reaction, which takes 30-60 s. Synchronization of the peristaltic pumps PI and P2 in the valveless impulse-response flow injection manifold depicted in Fig. 5.19.B by means of a timer enables kinetic measurements [62]. Following a comprehensive study of the effect of hydrodynamic and (bio)chemical variables, the sensor was optimized for monitoring urea in real biological samples. A similar system was used for the determination of penicillin by penicillinase-catalysed hydrolysis. The enzyme was immobilized on acid-base cellulose strips via bovine serum albumin similarly as in enzyme electrodes [63], even though the above-described procedure would have been equally effective. 

Since proteins contain a lot of acidic and basic side chains acting as weak acids and bases, respectively, proteins are buffering substances, too. If you mix buffer solutions with protein solutions, pH may be altered because the concentration of protein s buffering residues may exceed the capacity of the (chemical) buffer. For instance, bovine serum albumin contains 59 basic (Lys) and 99 acidic (59 Asp plus 40 Glu) residues per mole a solution of 10 mg/ml (1%) BSA contains 9 mM basic and 14.5 mM acidic residues, and phosphate-buffered saline (PBS) contains only 10 mM phosphate. As a consequence of this example (a) the concentration of the chemical buffer should be high enough to act as a buffer, (b) choose a chemical buffer the pK of which is nearby the pH to be stabilized, and (c) adjust the pH after all components are mixed. 

For the modification of the gold surface different chemical and biological substances (dodecanethiol, lectins, dextran sulfate DS, with the mass of 5 kDa and polyelectrolytes) were used. The mercaptane layer was formed in ethanol atlO" M concentration of thiol. Polyaniline hydrochloride (PAH), Aldrich , USA, was used to cover the transducer surface by a water insoluble polymer. Lectins from Phaseolus vulgaris (PLA), Solanum tuberosum (STA), Helix pomatia (HPA) and Tuberosum vulgaris (WGA) were immobilized on the surface pre-treated with dodecanethiol or PAH. These lectins were used for the immobilization of glycoproteins. Blocking of the free binding sites was carried out with 1% bovine serum albumin (BSA). 

Pore building, hydrophilic excipient bovine serum albumin (Sigma Chemical Company, St. Louis, MO) of high and low dissolution rates (the dissolution rate of the product could be reduced by special treatment) ... 

The protein used was crystalline bovine serum albumin (BSA) obtained from Armour Laboratories. Sodium dodecyl sulfate (SDS) was synthesized from pure dodecyl alcohol and chlorosulfonic acid, recrystallized, and washed with ethyl ether. Sulfuric acid was reagent grade purchased from the J. T. Baker Chemical Co. and used directly. Reagent grade potassium hydroxide purchased from the Mallinkrodt Co. was purified by foaming a concentrated solution, removing the foam, and using the solution directly. 

Bovine Serum Albumin. Since Polis et al. (1950) crystallized bovine serum albumin from whey and demonstrated that it was identical in all properties investigated to blood serum albumin, except in its electrophoretic behavior at pH 4.0, very little work has been done on this protein as isolated from milk. However, much work has been done on the protein isolated from bovine blood plasma. There is considerable evidence that serum albumin is heterogeneous. For example, Spencer and King (1971) have demonstrated several protein bands by electrophoretic focusing, with two major isoelectric components differing by one unit of charge. The chemical nature of this difference is not known. 

Other chiral immobilised stationary phases are available commercially, for example covalently bonded bovine serum albumin or chemically bonded l-hydroxyproline-Cu2 complexes to wide-bore Nucleosil (both from Macherey-Nagel). 

Protein was measured by the method of Lowry eit al (64). Crystalline bovine serum albumin (Sigma Chemical Company) served as a standard. 

We explored the detection and quantification of specific functional groups in proteins using quantitative specific chemical modifications that contain elements with high detection sensitivity. Fluorine was introduced specifically into Bovine Serum Albumin (BSA) by N-trifluoracetylation of the e-amino group of lysine using ethyl thiotrifluoracetate (47). The fluorine electron spectrum from N-trifluoracetylated BSA is shown in Figure 18. 

Figure 18. Fluorine Is spectrum from bovine serum albumin trifiuoroacetylated with ethyl thiotrifluoracetate. (Reproduced from Ref. 47. Copyright 1974, American Chemical Society.)...

Figure 15.10 Biocompatible microfabrication allows trapping of a single bacterium. (A, B) SEM images of a bovine serum albumin microcontainer. (C) SEM of a container after the entrance was plugged with a bacterium inside. (D) Sequence showing the container before (1) and immediately after (2) fabrication of a plug to trap the bacterium (arrow scale bar, 10 pirn.). Cell division eventually fills the trap with no loss of bacteria (3-6) (reprinted with permission from [17] 2007 American Chemical Society).

FIGURE 6.10 Van Deemter plots for capillary electrophoresis ( ) and microchip electrophoresis (o), where plate height (H) of TRITC-labeled bovine serum albumin is plotted vs. migration velocity (v) [174]. Reprinted with permission from the American Chemical Society. 

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