Albumin, bovine serum structure

They experimented with four other proteins as carriers rabbit serum albumin, bovine serum albumin, bovine fibrinogen fraction I, and bovine )8-globulin fraction III. The structurally related derivatives of DDT and malathion, DDA, and 0,0-dimethyl S-carboxy-carboxyethyl phosphoro-dithioate (malathion half ester), respectively, were used as the specific haptens attached to these carrier proteins. These compounds contain free carboxyl groups, which when they reacted with thionylchloride, provide a means of coupling of the hapten to the amino groups of the protein carrier. 

Structured proteins have also been investigated by thermal analysis [40,41], denaturing resulting in an endotherm which is readily detected by differential scanning calorimetry (DSC). DSC of recombinant resilin in the swollen state showed no transitions over a wide temperature range (25°C-140°C), further evidence of the absence of any strucmre. This is in contrast to the strucmred proteins wool and bovine serum albumin, which show denamration endotherms at 145°C and 62°C, respectively (Figure 9.6). 

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... 

The imidazolate bridged Cu/Zn bimetallic complex of the cryptand (13) was structurally characterized and shown to have a Cu-Zn distance of 5.93 A (native Cu, Zn-SOD 6.2 A).146 The complex shows some activity in the dismutation of superoxide at biological pH that is retained in the presence of bovine serum albumin. 

Na salts of ribonucleotide triphosphates (Roche or Sigma) bovine serum albumin RNase-free, 20 mg/ml (Roche) RNasin ribonuclease inhibitor, 40 U/ml (Promega) both bacteriophage T7 RNA polymerase and RNA Cap structure analog m7G(5/)ppp(5/)G are from BioLabs DNase-RNase-free (Roche) complete EDTA-free proteinase inhibitors cocktail (Roche) pyruvate kinase (PK) (Roche). 

Sulindac-Bovine-Serum-Albumin (BSA)] CONJUGATE STRUCTURES... 

Although the occurrence of six conserved cysteine residues, the spacing patterns of these residues, and possibly the pattern of disulfide structures are hallmarks of OBPs, the six-cysteine criterion alone is not sufficient to classify a certain protein as an olfactory protein [ 16]. It is important to demonstrate that an OBP is expressed only (or predominantly) in olfactory tissues. Evidence for their ability to bind odorants is also desirable, but not sine qua non. One of these criteria alone would not be enough to define a given protein as an OBP. For example, bovine serum albumin (BSA) binds to insect pheromones (Leal, unpublished data) and yet it is not an OBP because it not expressed in insect olfactory tissues. Conversely, a protein specific to antennae is not necessarily an OBP. There are other proteins that may be expressed in antennae but not in control tissues. Non-OBPs specifically accumulated in insect antennae have been previously detected (Ishida and Leal, unpublished data). Also, a glu-tathione-S-transferase has been reported to be expressed specifically in antennae of M. sexta [52]. 

That conclusion is supported and extended by the virtually simultaneous publication of Teale and Benjamin (1976). These investigators studied the oxidative regeneration of bovine serum albumin, assaying the extent of refolding immunochemically. Their results showed clearly that some parts of the molecule fold faster than others. Two fragments of albumin were tested for oxidative regeneration in the same way. Substantial return of native structure was seen in both fragments. 

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... 

J.R. Lu, T.J. Su, and R.K. Thomas Structural Conformation of Bovine Serum Albumin Layers at the Air-Water Interface Studied by Neutron Reflection. I. Colloid Interface Sci. 213, 426 (1999). 

Figure 7. Structure and location of the six regions of bovine serum albumin (BSA) and of human serum albumin (HSA) that we have shown to carry antigenic sites. It Is not Implied that the antigenic sites comprise the entire size of the regions shown, but rather that they fall within these regions. Reproduced with permission from Refs. 9, 10, and 11.

Another derivatization approach is reduction of the hydroperoxide, followed by structural characterization of the corresponding alcohol, which is usually easier to handle. Thus, the structure of amino acid hydroperoxides can be characterized more easily if, after having ascertained the hydroperoxide nature of the compound, it is reduced to the alcohol with NaBH4. The structure of three valine hydroperoxides obtained on y-radiation of bovine serum albumin, a tripeptide (31) or valine (34) was elucidated after reduction, hydrolysis (if necessary), chromatographic separation, and application of the usual MS and NMR methods on the individual hydroxy derivatives of valine. ... 

Rawel, H.M., Rohn, S., Kruse, H.P., and Kroll, J., Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid. Food Chem., 78, 443, 2002. 

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