فارسی
1
کشاورزی::
سرم آلبومین گاوی
Among the other food proteins, a-lactalbumin, bovine serum albumin (BSA) and caseins are studied to a lesser extent for their binding properties toward flavour compounds. a-Lactalbumin was found to bind ketones and aldehydes but with a poor flavour binding capacity compared to other whey proteins (Jasinski and Kilara, 1985).
The binding of vanillin to native BSA also exhibited two binding sites at pH 6.4 without any binding activity at pH 2.5 (Burova et al.
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2
عمومی::
سرم آلبومین گاوی
[00292] In the following tests, 3% BSA/PBS was used as a solvent for adjusting the concentration of an antibody, without otherwise specified.
The solution was removed, and a blocking buffer (3% bovine serum albumin (BSA)-PBS) was then dispensed at 270 �L/well, and the plate was allowed to stand at 4�C overnight.
After the solution was removed, a blocking buffer (3% bovine serum albumin (BSA)-PBS) was dispensed at 270 ?
, Peptides Nos. 1 to 12, or conjugates of these peptides with bovine serum albumin (BSA) or keyhole limpet hemocyanin (KLH), were each diluted with PBS cooled to 4�C to 1 �g/mL, and the resultant solution was dispensed to a plate at 50 �L/well and allowed to stand at 4�C overnight.
The concentration of the purified tau protein was determined by bicinchoninic acid (BCA) assay, using bovine serum albumin (BSA) as a standard sample.
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3
متالوژی::
آلبومین سرم گاوی
As a consequence of the enlargement of the mesopores after the thermal treatment for several days, it was possible to increase the BSA loading from 15%, assessed by the physical adsorption on the external surface of the material, to 27%,
This huge increment in pore diameter allowed the introduction of large pro- teins, such as bovine serum albumin (BSA) (Schmidt-Winkel et al. 1999), to be then released, as represented in Figure 2.10.
The influence of the pore volume was observed when quantifying the amount of BSA loaded into the network of cavities: the higher the pore volume, the greater the protein adsorption.
Thus BSA loading was increased from 15% in traditional SBA- 15 materials up to 24% in these new MCF materials (Vallet-Regí et al. 2008).
FIGURE 2.10 Representation of SBA-15 materials with enlarged pore diameter and pore volume to be able to load proteins such as bovine serum albumin.
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