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Aprotinine

Permeation enhancers are used to improve absorption through the gastric mucosa. Eor example, oral dehvery of insulin (mol wt = 6000) has been reported from a water-in-oH- emulsion containing lecithin, nonesterified fatty acids, cholesterol [57-88-5], and the protease inhibitor aprotinin [9087-70-1] (23). [Pg.141]

FIGURE 7.17 Separation of a complex mixture on Fractogel EMD BioSEC (S) with a column dimension of 1000 X 50 mm (Superformance glass column). The sample contained ferritin (I), immunoglobulin G (2), transferrin (3), ovalbumin (4), myoglobin (5), aprotinin (6), and vitamin B, (7). Five milliliters of the mixture was injected onto the column at a flow rate of 3 ml/min (eluent 20 mAI sodium phosphate buffer, 0.1 M NaCI, pH 7.2). [Pg.241]

Aprotinin. Aprotinin is a naturally occurring serine protease inhibitor, has found widespread applications either by the intravenous route or as a component of biological sealants, because of its ability to decrease blood loss, and, as a consequence, transfusion requirements. Anaphylactic reactions are mediated by IgG and IgE antibodies. The risk of anaphylactic reactions has been estimated between 0.5 and 5.8% when used intravenously during cardiac surgery, and at 5 for 100,000 applications when used as a biologic sealant [25]. Patients previously treated with this drug present an increased risk and any new administration should be avoided for at least 6 months following an initial exposure [25]. [Pg.186]

Dietrich W, Ebell A, Busley R. Boulesteix AL Aprotinin and anaphylaxis analysis of 12,403 exposures to aprotinin in cardiac surgery. Ann Thorac Surg 2007 84 1144. [Pg.189]

Gel Filtration. The lyophilized protein was redissolved in 50 mM phosphate buffer, pH 7.4 0.15 m NaCl 0.013 % sodium azide and loaded on a Superdex 75HR1030 column equilibrated with the same buffer. Elution was downward flow (0.15 ml/min) and 0.25 ml fi actions were collected. Fractions with pectin lyase activity were combined, dialyzed against distilled water and used in the next step. To estimate the molecular mass of PNL, the column was calibrated with standard proteins (Sigma MW-GF-70 Albumin, 66,000 Da Carbonic Anhidrase, 29,00 Cytochrome, 12,400 and Aprotinin, 6,500). The proteins were eluted in the conditions described above and their volumes (F ) were calculated fi om the peak maximum of the absorbance at 280 nm. The partition coefficient was obtained fi om the relationship where F, represents the bed volmne of column and F the void volume (which was calculated using blue dextran. Sigma). The molecular mass was determined using a standard curve of vs the logarithm of the molecular masses of the standards [28, 29]... [Pg.750]

Figure 4. Estimation of molecular weight by calibration of Superdex 75HR1030. Standard proteins 1, Albumin (66,000 Da) 2, Carbonic Anhidrase (29,000 Da) 3, Cytochrome c (12,400 Da) 4, Aprotinin, (6,500 Da). The line has been drawn using the equation Ig m = 5.01930882 -2.757789171 r = - 0.9965. Figure 4. Estimation of molecular weight by calibration of Superdex 75HR1030. Standard proteins 1, Albumin (66,000 Da) 2, Carbonic Anhidrase (29,000 Da) 3, Cytochrome c (12,400 Da) 4, Aprotinin, (6,500 Da). The line has been drawn using the equation Ig m = 5.01930882 -2.757789171 r = - 0.9965.
Figure 14. Effect of oral delivery of an insulin/polyacid matrix to diabetic rabbits on serum glucose, with and without adjuvants (sodium taurocholate, aprotinin). Figure 14. Effect of oral delivery of an insulin/polyacid matrix to diabetic rabbits on serum glucose, with and without adjuvants (sodium taurocholate, aprotinin).
A plasmin inhibitor such as aprotinin used for blood collection, while effective in inhibiting activation of plasminogen by urokinase, is ineffective against the ac-... [Pg.160]

Lottenberg R., Sjak-Shie N., Fazleabas A. T Roberts R. M. Aprotinin inhibits urokinase but not tissue-type plasminogen activator. Thromb Res 1988 49,549-56. [Pg.168]

FIGURE 6.6 Merck Chromolith monolithic RPLC column at 1 mL/min (top) and 2 mL/min with various injection volumes. Protein standards A = aprotinin, B = cytochrome C, C = carbonic anhydrase. [Pg.140]

Polymorphism and solvatomorphism are not, of course, limited to small molecules, and such phenomena can be observed in protein crystals as well. Two polymorphic forms of aprotinin have been identified, and the solubility of these studied in a variety of aqueous media [84], The needle polymorph was found to exhibit increased solubility with increased temperature (i.e., an endothermic heat of solution), while the solubility of the bipyramid form decreased by with increasing temperature (i.e., an exothermic heat of solution). The solubility curves crossed at 25 °C for a pH of 4.75, and hence one could obtain the desired crystal form through a judicious selection of crystallization temperature. [Pg.274]

Aprotinin Maize ubiquitin promoter/ pinll terminator Maize ubiquitin 5 intron, barley a-amylase LP Extracellular matrix of embryo (maize seeds) In T5 0.35% of extractable seed proteins 16... [Pg.96]

Encapsulation within an enteric coat (resistant to low pH values) protects the product during stomach transit. Microcapsules/spheres utilized have been made from various polymeric substances, including cellulose, polyvinyl alcohol, polymethylacrylates and polystyrene. Delivery systems based upon the use of liposomes and cyclodextrin-protective coats have also been developed. Included in some such systems also are protease inhibitors, such as aprotinin and ovomucoids. Permeation enhancers employed are usually detergent-based substances, which can enhance absorption through the gastrointestinal lining. [Pg.71]

Aungst BJ, Rogers NJ (1988a) Site dependence of absorption-promoting actions of laureth-9, Na salicylate, Na2EDTA, and aprotinin on rectal, nasal, and buccal insulin delivery. Pharm Res 5 305-308... [Pg.103]

Serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein, and plasmin Binding is reversible, with most aprotinin-protease complexes dissociating at pH>10or <3 Peptidase inhibitor... [Pg.204]

Aprotinin is a polypeptide consisting of a chain of 58 amino acid residues, which inhibits stoichiometrically the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin, and trypsin. Aprotinin is obtained from bovine tissues and purified by a suitable process. It is stored as a bulk solution or lyophilized powder. The amount of two related substances des-Ala-des-Gly-aprotinin and des-Ala-aprotinin is determined by CZE with a 100% analysis. The relative migration times are 0.98 for des-Ala-des-Gly-aprotinin and 0.99 for des-Ala-aprotinin, and the specified limits are 8.0 and 7.5%, respectively. [Pg.157]

Aprotinin Aprotinin injection USP Related substances Polypeptide na ... [Pg.158]


See other pages where Aprotinine is mentioned: [Pg.179]    [Pg.181]    [Pg.1113]    [Pg.1113]    [Pg.91]    [Pg.120]    [Pg.123]    [Pg.124]    [Pg.125]    [Pg.222]    [Pg.236]    [Pg.241]    [Pg.676]    [Pg.133]    [Pg.180]    [Pg.341]    [Pg.44]    [Pg.64]    [Pg.65]    [Pg.63]    [Pg.64]    [Pg.107]    [Pg.274]    [Pg.280]    [Pg.286]    [Pg.406]    [Pg.93]    [Pg.204]    [Pg.279]   
See also in sourсe #XX -- [ Pg.140 ]

See also in sourсe #XX -- [ Pg.133 ]

See also in sourсe #XX -- [ Pg.24 , Pg.524 ]

See also in sourсe #XX -- [ Pg.524 ]




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Aprotinin

Aprotinin

Aprotinin Heparin

Aprotinin Suxamethonium

Aprotinin Tubocurarine

Aprotinin allergic reactions

Aprotinin aminocaproic acid

Aprotinin anaphylactic reactions

Aprotinin blood transfusion

Aprotinin cardiopulmonary bypass

Aprotinin coronary artery bypass

Aprotinin death

Aprotinin inhibition

Aprotinin plasma concentrations

Aprotinin postoperative cardiac

Aprotinin renal function

Aprotinin surgery

Aprotinin tranexamic acid

Aprotinin, solution preparation

Aprotinine as protease inhibitor

Kallikrein-trypsin inhibitor - Aprotinin

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