Bovine serum albumin , aggregation

Yoshika, S., Asu, Y., Kojima, Sh. Determination of molecular mobility of lyophilized bovine serum albumin and gamma-globulin by solid-state H1 NMR and relation to aggregation-susceptibility. Pharm. Res. 13 (6), p. 926-930, 1996... 

Although resolution in SEC is relatively low as compared with other techniques (e.g., SDS-PAGE), it allows analysis of the native protein. Thus, we can obtain a glimpse into the tertiary or quaternary structure of the molecule. Indeed, proteins such as bovine serum albumin (BSA) are usually resolved into monomer, dimer, tetramer, etc., by SEC. Caution should be exercised, as aggregates can go... 

The synthetic polymeric components as well as their combinations with proteins such as human serum albumin (HSA), bovine serum albumin (BSA), human serum albumin/a-interferon mixtures (HSA-IFNa) and myoglobin (MYO) did not give any negative response to in vitro and in vivo biocompatibility tests, such as platelet aggregation, complement activation, acute toxicity, and acute thromboembolic potential. 

Su, R., Qi, W., He, Z., Zhang, Y. Jin, F. (2008). Multilevel structural nature and interactions of bovine serum albumin during heat-induced aggregation process. Food Hydro-colloids, 22, 995-1005... 

Triton X-100, EDTA, dithiothreitol and electrolyte protect enzyme in dilute solution and against denaturation by heat or extreme pH-values [12, 48] <2>, at low dithioerythritol concentrations enzyme tends to aggregate [5] <2>, bovine serum albumin, 1 mg/ml, stabilizes dilute enzyme solutions [5] <2>, diadenosine pentaphosphate, i.e. AP5A, stabilizes during preparative electrophoresis [7]... 

Fig. (3). Hemozoin Production Mediated by Bionucleating Templates. Representative polymerization assay with 50 pM of hemin in 2 ml acetate buffer (500 mM, pH 4.8) at 37° C. BNTI and BNTII were used in 1 and 2 nmol amounts. Chloroquine (CQ, 100 pM) was included with BNT I and BNT n in inhibition reactions. Polyhistidine and bovine serum albumin in approximately 1 and 2 nmol amounts were used in protein control experiments. The blank control was the acetate buffer above. Base line amounts of insoluble aggregate are consistent with those previously reported under similar conditions.

Yoshioka et al. [1.155] studied the mobility of protons by NMR in freeze-dried bovine serum albumin (BSA) and y-globulin (BGG) and its relation with aggregation susceptibility. The spin-spin relaxation time tSR of protons in BSA and BGG was measured as a function of the water content in the range 0.2-0.5g/g (g water/g protein) in both products. The increase in tSR and the increase in the aggregation susceptibility were strongly related. 

This review concentrates on chiral templates that transfer the chiral information in a ground state complex in solution, and it considers results published before the beginning of 2003. Reviews focusing on chiral auxiliaries, chiral sensitizers, CPL as well as on enantioselective photochemistry in the solid state, in confined media, or in molecular aggregates can be found elsewhere in this book. Moreover, it should be mentioned that this account deals with synthetic templates. Natural templates such as cyclodextrins, bovine serum albumin, and DNA will be accounted for separately. 

At the second critical pH (pH,, ), which is usually below the protein isoelectric point, strong electrostatic interaction between positively charged protein molecules and anionic polysaccharide chains will cause soluble protein/polysaccharide complexes to aggregate into insoluble protein/polysaccharide complexes. For negatively charged weak acid-based (e.g., carboxylic acid) polysaccharides like pectin, with the decrease of pH below the pKa of the polysaccharide, protein (e.g., bovine serum albumin (BSA))/polysaccharide (e.g., pectin) insoluble complexes may dissociate into soluble complexes, or even non-interacted protein molecules and polysaccharide chains, due to the low charges of polysaccharide chains as well as the repulsion between the positively charged proteins (Dickinson 1998). 

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