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Solution albumin

Inactivation and Removal of Viruses. In developing methods of plasma fractionation, the possibiHty of transmitting infection from human vimses present in the starting plasma pool has been recognized (4,5). Consequentiy, studies of product stabiHty encompass investigation of heat treatment of products in both solution (100) and dried (101) states to estabHsh vimcidal procedures that could be appHed to the final product. Salts of fatty acid anions, such as sodium caprylate [1984-06-17, and the acetyl derivative of the amino acid tryptophan, sodium acetyl-tryptophanate [87-32-17, are capable of stabilizing albumin solutions to 60°C for 10 hours (100) this procedure prevents the transmission of viral hepatitis (102,103). The degree of protein stabilization obtained (104) and the safety of the product in clinical practice have been confirmed (105,106). The procedure has also been shown to inactivate the human immunodeficiency vims (HIV) (107). [Pg.530]

Biomedical and Biotechnology. The use of mictocapsules for a variety of biomedical and biological appHcations has been promoted for many years (50,51). Several biomedical mictocapsule appHcations ate in clinical use or have approached clinical use. One appHcation is the use of air-fiUed human albumin mictocapsules as ultrasound contrast agents. Such mictocapsules, caUed mictobubbles, ate formed by ultrasonicating 5% albumin solutions to produce 4—10-)J.m diameter air-fiUed capsules (52). When injected the capsules act as a useful transpulmonary echo contrast agent (53) that has been approved for use in humans by the U.S. FDA. [Pg.324]

Shortly after the liquid-breathing expenment [f] was published, the same liquid was used to perfuse an isolated heart from an animal [6], by intermittent perfusion with typical aqueous buffer and fluorocarbon Then Sloviter [7] showed that an emulsion of this fluorocarbon liquid, made by ultrasonication with an albumin solution, could sustain the life of the brain of a rat as well as or better than perfusing... [Pg.1139]

Eiweiss-hsmen, n. albuminuria, -korper, m. albuminous substance, protein, -leim, m. albumin glue gluten protein. -Idsung, /. albumin solution, -nahrung, /, albuminous food, -papier, n. albuminized paper, eiweiss-reich, a. rich in albumin (or in protein), -spaltend, p.a. proteolytic. [Pg.126]

Figure 6 Effect of the increased rotational correlation time on the proton relaxivity of MP2269, a Gd111 chelate capable of noncovalent protein binding (Scheme 2). The lower NMRD curve was measured in water, whereas the upper curve was obtained in a 10%w/v bovine serum albumin solution in which the chelate is completely bound to the protein. The rotational correlation times calculated are rR=105ps in the nonbound state, and rR= 1,000 ps in the protein-bound state (t=35°C). For this chelate, the water exchange... Figure 6 Effect of the increased rotational correlation time on the proton relaxivity of MP2269, a Gd111 chelate capable of noncovalent protein binding (Scheme 2). The lower NMRD curve was measured in water, whereas the upper curve was obtained in a 10%w/v bovine serum albumin solution in which the chelate is completely bound to the protein. The rotational correlation times calculated are rR=105ps in the nonbound state, and rR= 1,000 ps in the protein-bound state (t=35°C). For this chelate, the water exchange...
The introduced THEOS did not bring about precipitation in protein solutions. This behavior differs from that observed with common silica precursors. For example, TEOS added in such small amounts caused precipitation. By using THEOS, we could prepare homogeneous mixtures. When its amount introduced into the albumin solution was less than 5 wt.%, there was no transition to a gel state (Table 3.1). A gradual increase in THEOS concentration resulted in a rise in the solution viscosity. The transition to a gel state took place as soon as a critical concentration was reached. Its value, as demonstrated in Ref. [Pg.96]

Albumin 5% and 25% concentrations are available. It takes approximately three to four times as much lactated Ringer s or normal saline solution to yield the same volume expansion as 5% albumin solution. However, albumin is much more costly than crystalloid solutions. The 5% albumin solution is relatively iso-oncotic, whereas 25% albumin is hyperoncotic and tends to pull fluid into the compartment containing the albumin molecules. In general, 5% albumin is used for hypovolemic states. The 25% solution should not be used for acute circulatory insufficiency unless diluted with other fluids or unless it is being used in patients with excess total body water but intravascular depletion, as a means of pulling fluid into the intravascular space. [Pg.162]

Hetastarch 6% has comparable plasma expansion to 5% albumin solution but is usually less expensive, which accounts for much of its use. Hetastarch should be avoided in situations in which short-term impairments in hemostasis could have adverse consequences (e.g., cardiopulmonary bypass surgery, intracranial hemorrhage), because it may aggravate bleeding due to mechanisms such as decreased factor VIII activity. [Pg.162]

A calibration graph should be prepared using standard albumin solutions ranging in concentration from 0.J to 2.0 gl ... [Pg.396]

Formulation Aranesp is formulated as a sterile, colorless, preservative-free protein solution for intravenous (IV) or subcutaneous (SC) administration. There are two formulations the polysorbate solution includes excipients such as polysorbate 80, sodium phosphate monobasic monohydrate, sodium phosphate dibasic anhydrous, and sodium chloride in water-for-injection while the albumin solution contains albumin, sodium phosphate monobasic monohydrate, sodium phosphate dibasic anhydrous, and sodium chloride in water-for-injection. The pH for both formulations is 6.2 + 0.2. [Pg.171]

The importance of the magnetic coupling is easily seen in Fig. 17 which shows two water proton MRD profiles for serum albumin solutions at the same composition (89). The approximately Lorentzian dispersion is obtained for the solution, and reports the effective rotational correlation time for the protein. The magnetic coupling between the protein and the water protons carries the information on the slow reorientation of the protein to the water spins by chemical exchange of the water molecules and protons between the protein and the bulk solution. When the protein is cross-linked with itself at the same total concentration of protein, the rotational motion of the protein... [Pg.315]

Both isoelectric albumin and its undissociated acid and basic salts are less solvated and imbibe less liquid than the ionised form thus the viscosity of an albumin solution will be least at the isoelectric point rising to more or less well defined maxima on each side, these maxima coinciding with the points of maximum dis-... [Pg.315]

Nickel-containing alloys are used in patients in joint prostheses, sutures, clips, and screws for fractured bones. Corrosion of these implants may lead to elevated nickel levels in the surrounding tissue and to the release of nickel into extracellular fluid (lARC 1990 Sunderman 1989a Sunderman et al. 1986, 1989c). Serum albumin solutions used for intravenous infusion fluids have been reported to contain as... [Pg.202]

AES is used in pharmacopoeial assays of (1) Na in albumin solution and plasma protein solution (2) K, Na and barium (Ba) in calcium acetate used to prepare dialysis solutions (3) Ca in adsorbed vaccines (e.g. diphtheria and tetanus). [Pg.125]

AAS is used in a number of limit tests for metallic impurities, e.g. magnesium and strontium in calcium acetate palladium in carbenicillin sodium and lead in bismuth subgallate. It is also used to assay metals in a number of other preparations zinc in zinc insulin suspension and tetracosactrin zinc injection copper and iron in ascorbic acid zinc in acetylcysteine lead in bismuthsubcarbonate silver in cisplatinum lead in oxyprenolol aluminium in albumin solution and calcium, magnesium, mercury and zinc in water used for diluting haemodialysis solutions. [Pg.130]

It is obtained from heat treated pooled human plasma. 100 ml of 20% human albumin solution is osmotic equivalent of 800 ml of whole blood. It draws and holds additional fluid from tissues. It can used irrespective of patient s blood group. For optimum benefit it should be used with electrolyte solutions. It does not interfere with coagulation and there is no risk of sensitization. [Pg.199]

Fig. 29.1 SCN hemosorbent capacity towards unconjugated bilirubin adsorbed from (a) phosphate buffer solution and (b) 3% human serum albumin solution. SCN is one of the most efficient conventional hemosorbents based on activated carbon [4]... Fig. 29.1 SCN hemosorbent capacity towards unconjugated bilirubin adsorbed from (a) phosphate buffer solution and (b) 3% human serum albumin solution. SCN is one of the most efficient conventional hemosorbents based on activated carbon [4]...
The use of HSGD sorbents allows efficient purification of albumin from unconjugated bilirubin (Fig. 29.7). Upon eontaet of loaded albumin solution with HSGD the melting eurve of albumin normalizes and the molecular ratio of ligand to carrier falls by 300 times (Fig. 29.7) [7]. Normalization of the melting curve of albumin after its purifieation with HSGD from a mixture of hepatie toxins is shown in Fig. 29.8. [Pg.296]

Dosage form Aranesp is formulated as a sterile, colorless, preservative-free protein solution. Single-dose vials are available containing 25, 40, 60, 100, or 200pg darbepoetin in a 1ml solution. Two formulations are available one contains polysorbate solution and the other contains albumin solution. [Pg.156]

Human plasma has a colloid osmotic pressure of 3.6 kPa, of which 2.8 kPa is contributed by albumin. Volume-for-volume, 4.5% albumin is approximately four times more effective in expanding the plasma volume than crystalloid solutions, and the effect lasts 6-8 hours, compared to only 15-20 min with crystalloids. Although popular in the past as volume expanders, albumin solutions have fallen into disfavour. They are prepared from pooled human plasma, with all the inherent risks of pooled blood products. Albumin can cause adverse reactions, similar to other transfusion reactions, such as chills, urticaria, and vasodilatation. These may be caused by organic or inorganic substances formed during the processing... [Pg.288]

Parsons, D.L. (1982). Fluorescence stability of human albumin solutions. J. Pharm. Sci., 71, 349-351. [Pg.177]

Albumin solution contains 2.5mg/mL albumin (human) 2.23mg/mL sodium phosphate monobasic monohydrate ... [Pg.456]

The osmotic pressure of salt-free (electrodialyzed) bovine serum albumin solutions was measured at pH = 5.37 ( ). At this pH the net charge of the protein molecules is zero. The following data were obtained in different runs ... [Pg.143]

Albumin solutions (1, 2, and 5wt%) are continuously ultrafiltered through a flat plate filter with a channel height of 2 mm. Under cross-flow filtration with a transmembrane pressure of 0.5 MPa, steady-state filtrate fluxes (cm min ) are obtained as given in Table P9.2. [Pg.152]

The result was that albumin passivation came into vogue for sometime. In fact, artificial kidneys and blood oxygenators were often treated with albumin solutions prior to clinical use 118,119). There is considerable evidence that such pre-treatment did indeed result in decreased platelet adhesion and activation for short periods, perhaps up to several hours, but that the effect was relatively short-lived. [Pg.45]

As in any pharmaceutical batch operation, batch uniformity is paramount. Studies by Greiff [7] have shown that when lyophilizing a 3-ml volume of a 2% serum albumin solution in a 10-ml-tubing vial there is a measurable effect of... [Pg.343]

Fig. 1.82.2. Water vapor partial pressure divided by total pressure as a function of time of5% bovine serum albumin solution (Figure 3 from [1.137])... Fig. 1.82.2. Water vapor partial pressure divided by total pressure as a function of time of5% bovine serum albumin solution (Figure 3 from [1.137])...

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See also in sourсe #XX -- [ Pg.272 ]




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