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Human albumin solution

Albumin solution, human (PhEur 2005) Human albumin solution is an aqueous solution of protein obtained from plasma. Separation of the albumin is carried out under controlled conditions so that the final product contains not less than 95% albumin. Human albumin solution is prepared as a concentrated solution containing 150-250 g/L of total protein or as an isotonic solution containing 35-50 g/L of total protein. A suitable stabilizer against the effects of heat such as sodium caprylate (sodium octanoate) or N-acetyltryptophan or a combination of these two at a suitable concentration, may be added, but no antimicrobial preservative is added at any stage during preparation. The solution is passed through a bac-teria-retentive filter and distributed aseptically into sterile containers, which are then closed so as to prevent contamination. The solution in its final container is heated to 60 1.0°C and maintained at this temperature for not less than 10 hours. The containers are then incubated at 30-32°C for not less than 14 days or at 20-25°C for not less than 4 weeks and examined visually for evidence of microbial contamination. [Pg.17]

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]

Most frequently, binding protein is added to the incubation mixtures as either serum or purified serum albumin. With human serum albumin, at equilibrium, the acceptor substrate will largely be protein-bound, when the bilirubin albumin molecular ratio is smaller than one (the dissociation constant of the first binding site of purified human serum albumin is approximately 7 X 10 M with 2 X 10 M for two additional binding sites) (J2). The first binding site of albumin, measured with rat serum, has a dissociation constant of about 5 X 10" M (M8). The unbound fraction will normally not exceed the very low solubility of the pigment. Addition of albumin to an alkaline solution of bilirubin, or its addition immediately after neutralization, prevents colloid formation, if the bilirubin albumin molecular ratio is smaller than one (B25). However, colloidal bilirubin, once formed, cannot be redissolved by the addition of albumin (B26). [Pg.250]

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]...
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]

Human albumin solutions and other biological products intended for human use may contain aluminum because aluminum compounds are used in their manufacture or as a result of contamination. In albumin products, aluminum is generally introduced as a contaminant from filters, filter aides, buffer solutions, anticoagulants, as well as the container itself. Aluminum levels in a 5% pooled human albumin solution was 0.507 g/mL (Progar et al. 1996). [Pg.235]

L.R. Pierce, et al., Hemolysis and renal failure associated with use of sterile water for injection to dilute 25% human albumin solution. Am. J. Health Sys. Pharmacol. 55 1057, 1062, 1070, 1998. [Pg.376]

The next day the patient had decreased respiratory rate, became tired with falling blood sugar and acidosis. She had acute renal failure with urine output <30 mL/h and was in fluid overload. The doctors started her on terlipressin 2 mg q.d.s. and HAS (Human Albumin Solution) 20% to maintain central venous pressure 8-12 mmHg and prevent hepatorenal syndrome. Terlipressin is a prodrug for vasopressin. [Pg.345]

In addition to spironolactone, ascites can be managed by paracentesis. That is the removal ( tapping ) of ascitic fluid from the peritoneal cavity under aseptic conditions. A colloid (human albumin solution (20%)) is infused (40 mL (8 g of albumin) per litre of ascites drained) intravenously during paracentesis, in order to prevent intravascular volume depletion and the onset of renal failure. Following paracentesis, ascites recurs in the majority (93%) if diuretic therapy is not reinstituted, but recurs in only 18% of patients treated with... [Pg.351]

Human albumin solution has proved extremely reliable, especially when used in conjunction with crystalloid infusions. (Synthetic iso-oncotic colloids should be avoided as far as possible because of their negative effects on coagulation and kidney function.)... [Pg.351]

Matejtschuk, P. et al., Produchon of human albumin solution a continually developing coUoid, Br. J. Anasth., 85, 887-895, 2000. [Pg.425]

The fluid volume and protein removed by plasmapheresis must be replaced. Among the solutions available for replacement therapy are fresh frozen plasma and human albumin solutions. [Pg.2848]

Bunn F, Lefebvre C, Li Wan Po A, Li L, Roberts I, and Schierhout G. 2000. Human albumin solution for resuscitation and volume expansion in critically ill patients. The Albumin Reviewers. Cochrane Database Syst ReviCDOOi 208. [Pg.41]

BP Human albumin solution PhEur Albumin human solutio USP Albumin human... [Pg.16]

Albuconn albumin human solution Albuminar Albumisol Albuspan Albutein Buminate human serum albumin normal human serum albumin Plasbumin plasma albumin Pro-Butnin Proserum. [Pg.16]

Albumin solutions are manufactured from pooled plasma. They can contain other plasma constituents, such as heme compounds, prekalli-krein, endotoxins, bradykinin and bilirubin, in sufficient concentrations to cause clinical effects (Pulimood Park 2000). Some batches of human albumin have been shown to induce the expression of adhesion molecules on endothelial cells in vitro (Nohe et al 1999), which could result in activation of the immune system in vivo. Despite appropriate precautions during the manufacturing process, there is always a theoretical chance of transmission of disease with any biological product. [Pg.341]

Two formulations contain excipients as follows polysorbate solution contains 0.05 mg of polysorbate 80, 2.12 mg of sodium phosphate monobasic monohydrate, 0.66 mg of sodium phosphate dibasic anhydrous, and 8.18 mg of sodium chloride in water for injection, LISP (per 1 mL) at pH 6.2 + 0.2. Albumin solution contains 2.5 mg of albumin (human), 2.23 mg of sodium phosphate monobasic monohydrate, 0.53 mg of sodium phosphate dibasic anhydrous, and 8.18 mg of sodium chloride in water for injection, LISP (per 1 mL) at pH 6.0 + 0.3. [Pg.339]

Albumin is produced from human plasma by the alcohol fractionation method according to Cohn. The albumin is then controlled for the absence of antibodies against HIV, HCV and hepatitis B surface antigen (HBsAg). Furthermore, the albumin solution is kept at 60° C for 10 hours to inactivate HIV and hepatitis viruses. [Pg.69]

Albumin solutions prepared from human placentas may contain alkaline phosphatase and cause hyperphosphatasemia in the recipient (Ml, N2, P28). [Pg.217]

Simple systems (with a single defined additive) were produced with each of the following materials. Calf thymus DNA, polymerized, was obtained from Sigma. Protein sources were prepared in-house and subsequently dialyzed into low salt solutions. Human serum albumin and immunoglobulin G (IgG) were plasma-derived. Human immunoglobulin M (IgM) was produced by tissue culture fermentation and purified. A defined complex system consisted of both albumin and IgM together. An undefined complex system was set up with an intermediate material of Cohn plasma fractionation containing alpha-1 antitrypsin (alpha-1), albumin, and other contaminants. [Pg.97]

Effect of pH. Comparing Figures 3.35 and 3.36, both showing flux data on human albumin solutions, it will be seen that the gel concentration is 28% in one case and 45% in the other. This reflects the difference in solubility of proteins for different conditions such as pH. [Pg.173]

Leach CN JR and Sundeeman FW Je. (1985) Nickel contamination of human serum albumin solutions. N Engl J Med 313 1232. [Pg.861]

Figure 1. Teflon, exposed to human albumin solution, 2500 mg/dl, for 1 hr at room temperature. Air drying and partial gold decoration TEM technique were employed. (Reproduced with permission from Ref. 4. Copyright 1977 American Society for Artificial Internal Organs.)... Figure 1. Teflon, exposed to human albumin solution, 2500 mg/dl, for 1 hr at room temperature. Air drying and partial gold decoration TEM technique were employed. (Reproduced with permission from Ref. 4. Copyright 1977 American Society for Artificial Internal Organs.)...

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Human albumin

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