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Albumin amino acids

Formulation strategies for stabilization of proteins commonly include additives such as other proteins (e.g., serum albumin), amino acids, and surfactants to minimize adsorption to surfaces. Modification of protein structure to enhance stability by genetic engineering may also be feasible, as well as chemical modification such as formation of a conjugate with polyethylene glycol. [Pg.405]

Brown, J. R. 1977. Serum albumin Amino-acid sequence. In Albumin Structure, Function, and Uses. V.M. Rosenoer, M. Oratz and M.A. Rothschild (Editors). Pergamon Press, New York. [Pg.152]

Carballal S, Alvarez B, Turell L, Both H, Freeman BA, Radi R (2007) Sulfenic acid in human serum albumin. Amino Acids 32 543-551... [Pg.53]

One of the critical factors in excipient selection and concentration is the effect on preferential hydration of the biopharmaceutical product [53, 54], Preferential hydration refers to the hydration layers on the outer surface of the protein and can be utilized to thermodynamically explain both stability enhancement and denatur-ation. Typical excipients used in protein formulations include albumin, amino acids, carbohydrates, chelating and reducing agents, cyclodextrins, polyhydric alcohols, polyethylene glycol, salts, and surfactants. Several of these excipients increase the preferential hydration of the protein and thus enhance its stability. Cosolvents need to be added in a concentration that will ensure their exclusion from the protein surface and enhance stability [54], A more comprehensive review of excipients utilized for biopharmaceutical drug products is available elsewhere [48],... [Pg.20]

Henkin Rl. 1974. Metal-albumin, amino acid interactions Chemical and physiological interrelationships. In Friedman M, ed. Chemical and physiological interrelationships in protein-metal interactions. New York, NY Plenum Press, 299-328. [Pg.191]

Proteias, amino acids bonded through peptide linkages to form macromolecular biopolymers, used as chiral stationary phases for hplc iaclude bovine and human semm albumin, a -acid glycoproteia, ovomucoid, avidin, and ceUobiohydrolase. The bovine semm albumin column is marketed under the name Resolvosil and can be obtained from Phenomenex. The human semm albumin column can be obtained from Alltech Associates, Advanced Separation Technologies, Inc., and J. T. Baker. The a -acid glycoproteia and ceUobiohydrolase can be obtained from Advanced Separation Technologies, Inc. or J. T. Baker, Inc. [Pg.66]

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]

Amino acid CoUagen Elastin Keratin Albumin... [Pg.81]

Casein. Milk contains proteins and essential amino acids lacking in many other foods. Casein is the principal protein in the skimmed milk (nonfat) portion of milk (3—4% of the weight). After it is removed from the Hquid portion of milk, whey remains. Whey can be denatured by heat treatment of 85°C for 15 minutes. Various protein fractions are identified as a-, P-, and y-casein, and 5-lactoglobulin and blood—semm albumin, each having specific characteristics for various uses. Table 21 gives the concentration and composition of milk proteins. [Pg.370]

Biliverdin is an early product of catabohsm and on reduction yields bilirubin. The latter is transported by albumin from peripheral tissues to the hver, where it is taken up by hepatocytes. The iron of heme and the amino acids of globin are conserved and reutilized. [Pg.284]

Mature human albumin consists of one polypeptide chain of 585 amino acids and contains 17 disulfide bonds. By the use of proteases, albumin can be subdivided into three domains, which have different functions. Albumin has an ellipsoidal shape, which means that it does not increase the viscosity of the plasma as much as an elongated molecule such as fibrinogen does. Because of its relatively low molecular mass (about 69 kDa) and high concentration, albumin is thought to be responsible for 75-80% of the osmotic pressure of human plasma. Electrophoretic smdies have shown that the plasma of certain humans lacks albumin. These subjects are said to exhibit analbuminemia. One cause of this condition is a mutation that affects spUcing. Subjects with analbuminemia show only moderate edema, despite the fact that albumin is the major determinant of plasma osmotic pressure. It is thought that the amounts of the other plasma proteins increase and compensate for the lack of albumin. [Pg.584]

Human serum albumin 582 amino acids 17 disulphide bridges Yeast Plasma replacement therapy Normally obtained from plasma but now concern over potential contamination with AIDS virus... [Pg.464]

Some work has been completed on reaction of proteins with nitrite followed by hydrolysis and analysis for amino acids It has been shown that 3-nitrotyrosine and 3,4-dihydroxyphenylalanine are formed from bovine serum albumin when nitrosation occurs under conditions similar to those found in the human stomach (36), Direct demonstration that nitrite reacts with protein has been made by using NaN02 with bovine serum albumin (pH 5.5, 20 C and 200 ppm nitrite). A 60% loss of the originally added nitrite was observed in one week and nearly half of the nitrite (labelled %) could be recovered from the protein. Similar work with myosin revealed that 10-20% of the incorporated label was present as 3-nitrotyro-sine (J7). [Pg.297]

The property of thermal, reversible gelation is obtained by the addition of water-soluble proteins and protein degradation products to an aqueous solution of poly (vinyl alcohol) 2). Protein products such as albumin, gelatin, glue, a-amino acids, and their condensation products—diketopiperazines—may be used. A typical formulation for the preparation of a thermally reversible gel is ... [Pg.15]

Bovine serum albumin covalently bonded to silica and a-acid glycoprotein immobilized on silica have been used to resolve a wide range of acidic and basic drugs and amino acid derivatives [807-810]. Because of their complex structures, however, the... [Pg.969]

There is a wide variety of commercially available chiral stationary phases and mobile phase additives.32 34 Preparative scale separations have been performed on the gram scale.32 Many stationary phases are based on chiral polymers such as cellulose or methacrylate, proteins such as human serum albumin or acid glycoprotein, Pirkle-type phases (often based on amino acids), or cyclodextrins. A typical application of a Pirkle phase column was the use of a N-(3,5-dinitrobenzyl)-a-amino phosphonate to synthesize several functionalized chiral stationary phases to separate enantiomers of... [Pg.12]

Membranes offer a format for interaction of an analyte with a stationary phase alternative to the familiar column. For certain kinds of separations, particularly preparative separations involving strong adsorption, the membrane format is extremely useful. A 5 x 4 mm hollow-fiber membrane layered with the protein bovine serum albumin was used for the chiral separation of the amino acid tryptophan, with a separation factor of up to 6.6.62 Diethey-laminoethyl-derivatized membrane disks were used for high-speed ion exchange separations of oligonucleotides.63 Sulfonated membranes were used for peptide separations, and reversed-phase separations of peptides, steroids, and aromatic hydrocarbons were accomplished on C18-derivatized membranes. [Pg.65]

Albumin and amino acid loss Muscle wasting Increased adipose tissue Fibrin formation in dialysate... [Pg.398]

The N-terminal peptide fragment of des-angiotensinogen Val-Ile-His-Asn contains two strongly hydrophobic amino acid residues on the N-terminal site of His-3. The potentiometric data have shown that the NiH.2L complex with this albumin-like sequence is more than two orders of magnitude more stable than the respective complex with Gly-Gly-His.1744 The NMR-based molecular structure has shown that the side chains of Val-1 and lie-2 form a well-ordered hydrophobic fence (Figure 21) shielding one side of the coordination plane from the bulk of... [Pg.408]


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