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Structure of Bovine Serum Albumin

A considerable amount of information is available on the reversible, pH-dependent molecular conformational alterations which occur in both bovine and human serum albumins. This work has yielded valuable knowledge regarding the structural organization of the albumin molecule and has been instrumental in devising conditions and procedures for the enzymatic fragmentation of the protein and is therefore pertinent to an immunochemical consideration. [Pg.225]

Serum albumin exists in a compact form between pH 4.3 and 10.5 but undergoes conformational expansions below pH 4.3 and above pH 10.5 (Tanford et al., 955a,b Yang and Foster, 1954 Bro et al., 1955 Weber, 1952). Conformational transitions not accompanied by molecular expansion also occur, nhmely the N-F transition between pH 4.8 and 3.9 and the neutral transition, N-B, observed between pH 7 and 9 (Leonard etal., 1963). [Pg.225]


Figure 3.7. Primary structure of Bovine Serum Albumin. (From Brown 1975, 1977 Reed et al. 1980 Eigel et al 1984. Reprinted with permission of the American Dairy Science Association.)... Figure 3.7. Primary structure of Bovine Serum Albumin. (From Brown 1975, 1977 Reed et al. 1980 Eigel et al 1984. Reprinted with permission of the American Dairy Science Association.)...
The three-dimensional structure of bovine serum albumin has not been determined. Bovine serum albumin residues 126-144 (17-Amino-Acid Bovine Serum Albumin Peptide, ABBOS) have been reported to be responsible for the autoimmune reaction directed against pancreatic islet cells causing diabetes (Karjalainen et al. 1992). This remains controversial (Knip 2003, Persaud and Barranco-Mendoza 2004) but removal of this epitope as well as IgE binding is often an objective in producing infant formulas. [Pg.198]

B. X. Huang, H.-Y. Kim and C. Dass, Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry, J. Am. Soc. Mass. Spectrom., 15(8) 1237-1247 (2004). [Pg.89]

Moriyama Y, Kawasaka Y, Takeda K. Protective effect of small amounts of sodium dodecyl sulfate on the helical structure of bovine serum albumin in thermal denaturation. J Colloid Interface Sci 2003 257(1) 41 6. [Pg.291]

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. [Pg.1157]

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. [Pg.78]

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). [Pg.102]

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. 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. ... [Pg.691]

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... [Pg.150]

While gelation temperature Is usually considered a characteristic property of a given protein system, the heating conditions required for gel formation may be Interrelated to all of the previously mentioned factors. It has been observed that WPG dispersions In 0.2 M NaCl will gel at 75 C while a temperature of 90 C Is required to gel WPG dispersions In distilled water (1). Heating time, at a specific temperature, required to form a protein gel structure Is generally considered to decrease with Increased protein concentration. Alteration of heat treatment conditions affects the gel s macroscopic and microscopic structural attributes. This has been dramatically shown by Tombs (A) with electromlcroscoplc evaluation of bovine serum albumin gels. [Pg.144]

Due possibly to the above mentioned heterogeneity, there is some variability with regard to the conclusions reached by various workers concerning the structure and configuration of bovine serum albumin. Brown (1977) proposed two possible models based on the primary sequence of the protein. He demonstrated that the molecule could possess a triple domain structure with three very similar domains residues 1-190, 191-382, and 383-582. Each domain could then consist of five helical rods of about equal length arranged either in a parallel or an antiparallel manner. His second model consisted of the following (1) a lone subdomain (1-101) (2) a pair of antiparallel subdomains, with their hydrophobic faces toward each other (113-287) (3) another pair of subdomains (314-484) and (4) a lone subdomain (512-582). These structures are supported by the observed helical content of bovine... [Pg.118]

The elution pattern in IEC results from the charge distribution on the folded chain. Therefore, IEC was used for indication, whether the native structure of the protein had been affected by previous RPC or not. Ribonuclease was found to retain its native structure, whereas bovine serum albumin, horse radish peroxidase, and ovalbumin were much altered through RPC on a C 18 column with a gradient water/ (ethanol-butanol 80 20) containing 0.012 M HC1 in both eluent components 59>. [Pg.182]

Figure 9. Molecular arrangements in aqueous precipitates of bovine serum albumin and lecitnin-cardiolipin (14). Center lipid bilayers and left ana right two alternative structures of the precipitates based on the x-ray diffraction spacings. Figure 9. Molecular arrangements in aqueous precipitates of bovine serum albumin and lecitnin-cardiolipin (14). Center lipid bilayers and left ana right two alternative structures of the precipitates based on the x-ray diffraction spacings.
Wen et al. (1994) investigated the Raman optical activity of poly-L-lysine both as the random coil and the a-helix. They compared these spectra to the spectra of bovine serum albumin and insulin and arrived at the conclusion that tertiary structure of proteins can be readily deduced from the ROA spectra. [Pg.571]

Shablakh et al. (1984) investigated the dielectric properties of bovine serum albumin and lysozyme at different hydration levels, at low frequency. Besides a relaxation attributed to the electrode—sample interface, they detected a further bulk relaxation that can be confused with a d.c. conduction effect. The latter relaxation was explained by a model of nonconductive long-range charge displacement within a partially connected water structure adsorbed on the protein surface. This model has nonconventional features that differ from the assumptions of other more widely accepted models based on Debye relaxations. [Pg.68]

Spectrometry (MS) to follow structural changes associated with the degradation of bovine serum albumin (BSA) in seawater. BSA was degraded rapidly in seawater and enzymatic attack occurred at a variety of sites on this protein. Based on these results the authors concluded that either non-specific proteases or a diverse collection of specific proteases were abundant in seawater. Consistent with these findings, the signature of HMWDOM and proteins isolated from HMWDOM indicate that dissolved proteins are turning over more rapidly than bulk HMWDOM (Meador et ai, 2007). [Pg.130]

As an illustration, the rotatory dispersions shown in Fig. 1 have been replotted in Fig. 2 in a manner that yields linear behavior when the simple Drude equation is valid. It is seen that the disordered forms of the three substances do yield straight lines conforming with Eq. (10). The native form of bovine serum albumin does likewise, but the two purely helical structures, in contrast, exhibit distinct curvature. [Pg.411]


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