Bovine plasma protein

Figure B3.1.4 A 15% SDS-pdyacrylamide gel assayed for proteinase inhibitors. (A) Gel stained with Coomassie brilliant blue for total protein. (B) Gel assayed for serine-proteinase inhibitory activity against trypsin. Food-grade proteinase inhibitors used in surimi manufacture were assayed. Lane 1, whey protein concentrate. Lane 2, bovine plasma proteins. Lane 3, egg white. Each lane contains 15 pg protein. Lane M, molecular weight standards. The dark bands in (B) indicate proteins with proteinase inhibitory activity. Numerous proteins in egg white (lane 3) are shown to have inhibitory activity against trypsin. Adapted from Weerasinghe (1995).

Kisiel W, Canfield WM, Ericsson LN, Davie EW. Anticoagulant properties of bovine plasma protein C following activation by thrombin. J Biol Chem 1977 16 5824-583 I. 

Bovine Plasma Protein Adsorption onto Radiation-Grafted Hydrogels Based on Hydroxy ethyl Methacrylate and N-Vinyl-pyrrolidone... 

Utilisation of these ingredients has been investigated in the baking industry. Khan et al. (1979) used bovine plasma protein isolate (96% protein) to replace wheat flour in bread, or as a substitute for egg white... 

History. Methods for the fractionation of plasma were developed as a contribution to the U.S. war effort in the 1940s (2). Following pubHcation of a seminal treatise on the physical chemistry of proteins (3), a research group was estabUshed which was subsequendy commissioned to develop a blood volume expander for the treatment of military casualties. Process methods were developed for the preparation of a stable, physiologically acceptable solution of alburnin [103218-45-7] the principal osmotic protein in blood. Eady preparations, derived from equine and bovine plasma, caused allergic reactions when tested in humans and were replaced by products obtained from human plasma (4). Process studies were stiU being carried out in the pilot-plant laboratory at Harvard in December 1941 when the small supply of experimental product was mshed to Hawaii to treat casualties at the U.S. naval base at Pead Harbor. On January 5, 1942 the decision was made to embark on large-scale manufacture at a number of U.S. pharmaceutical plants (4,5). 

Marsh MM. Spectropolarimetric studies on proteins. Bovine plasma albumin and insulin. J Am Chem Soc 1962 84 1896-900. 

Sawada and coworkers [25-27] studied the iso-pH 7.4 MDCK permeabilities of very lipophilic molecules, including chlorpromazine (CPZ) [25], These authors included 3% wt/vol bovine serum albumin (BSA) on the apical (donor) side, and 0.1-3% BSA on the basolateral (acceptor) side, and found that plasma protein binding greatly affected the ability of molecules to permeate cellular barriers. They observed cell tissue retention of CPZ ranging from 65 to 85%, depending on the... 

Weekes J et al. Bovine dilated cardiomyopathy proteomic analysis of an animal model of human dilated cardiomyopathy Electrophoresis 1999 20 898-906. Doherty NS et al. Analysis of changes in acute phase plasma proteins in an acute inflammatory response and in rheumatoid arthritis using two-dimensional gel electrophoresis. Electrophoresis 1998 19 355-363. 

Cows and calves fed low-zinc diets of 25 mg Zn/kg ration showed a decrease in plasma zinc from 1.02 mg/L at start to 0.66 mg/L at day 90 cows fed 65 mg Zn/kg diet had a significantly elevated (1.5 mg Zn/L) plasma zinc level and increased blood urea and plasma proteins (Ram-achandra and Prasad 1989). Biomarkers used to identify zinc deficiency in bovines include zinc concentrations in plasma, unsaturated zinc-binding capacity, ratio of copper to zinc in plasma, and zinc concentrations in other blood factors indirect biomarkers include enzyme activities, red cell uptake, and metallothionein content in plasma and liver (Binnerts 1989). 

Parent drug is bound to bovine and human plasma proteins to an extent of 89 - 96 % (in vitro concentration range 0.2 -80 pg/ml) and exerts a pronounced affinity to various tissues. 

FlC. 9. Nonparallel regeneration of the functions for bilirubin binding and fatty acid binding in bovine plasma albumin. The oxidative regeneration of reduced albumin was carried out at protein concentrations of 1 ft,M at 25°C in 0.10 M Tris-chloride buffer, pH 8.0, containing 1 mM EDTA and 1 mM reduced and 0.10 mM oxidized glutathione (Johanson et al, 1977, 1981). 

Prepare competitor protein buffer detergent solution 4 mg/mL normal goat globulin or other competitor protein, (such as fetal calf serum, bovine serum albumin, bovine plasma, and so forth), and 0.1% saponin (Sigma, St. Louis, MO) in phosphate-buffered saline (NGG-sap-PBS). 

Kraak et al. (38) reported the first ACE application to study drug binding to a plasma protein. They used the model system warfarin-human serum albumin (HSA) to compare the suitability of the Hummel-Dreyer, frontal analysis, and vacancy peak methods. A more methodologically intended paper from Erim and Kraak (39) used VACE to study the displacement of warfarin from bovine serum albumin (BSA) by furosemide and phenylbutazone. They concluded that VACE is especially suited to examining competitive properties of simultaneously administered compounds toward a given protein-drug system. 

If we consider that cell adhesion under biological circumstances is mainly brought about with the aid of preadsorbed protein on the material s surface, we may explain the unique behavior of amino-containing materials against the cell-adhesion process in terms of the reduced residence-time of protein molecules at the interface. Actually, a recent study [129] revealed that the surface of polyamine-gra/t-polystyrene copolymer (SA) containing 6 wt.% polyamine portion exhibited a minimal adsorptive property against bovine plasma fibronectin (FN) and vitronectin (VN), both of which are known to mediate cell-adhesion processes. 

Albumin. Investigation into the safety of bovine plasma for clinical use was undertaken in the early 1940s in anticipation of wartime need (26). Using modem protein chemistry methods, including electrophoresis and ultracentrifugation, it was shown that most of the human adverse reactions to blood substitutes were caused by the globulin fraction and that albumin was safe for parenteral use. Human albumin is now used extensively as a plasma expander in many clinical settings. 

Size measurements can be done to study the interaction of polymeric micelles with biological media (Jones and Leroux, 1999). For instance, PERP -bPEO micelles were found to maintain their initial size in the presence of antibodies and bovine serum albumin, suggesting the apparent absence of interaction with plasma proteins (Kabanov et al., 1992). 

Malonaldehyde (MA) is a major end product of oxidizing or rancid lipids and it accumulates in moist foodstuffs (6). Several MA-protein systems have been studied. Chio and Tappel combined RNAase and MA to demonstrate fluorescence attributed to a conjugated imine formed by crosslinking two e-amino groups with the dialdehyde (7). Shin studied the same reaction and found it to be dependent on pH and reactant concentrations (8). Crawford reported the reaction between MA and bovine plasma albumin (BPA) also to be pH dependent, and of first order kinetics with a maximum rate near pH 4.30. At room temperature 50-60% of the e-amino groups were modified—40% in the first eight hours, the remainder over a period of days (9). 

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