Serum components albumin

Prepare cell or tissue extracts by standard procedures (see Note 3). Wash cultured cells or tissues well with PBS prior to preparation of extract to remove serum components (albumin binds to retinoic acid). Buffers containing high salt concentrations (0 3-0.6 M KCl) are usually used to ensure removal of receptor from DNA. Determine protein concentrations of all samples, store in aliquots at -80°C, and avoid freeze-thawing more than once. 

Whilst growth factors in the serum provide specific proliferative stimuli, studies with cultured cells have indicated other important components for cell proliferation [18]. For example, insulin is required to facilitate glucose and amino-acid uptake, and transferrin, which binds iron, makes it available to the cell. Serum is also believed to supply trace elements such as selenium, copper and zinc as well as fatty acids important for cell growth. Some serum components such as ascorbate, a-tocopherol, caeruloplasmin and albumin may serve important antioxidant functions [19]. 

Use a syringe and place a small drop of that dye mixture to the side along one edge of the cellulose acetate strip at the same place that you spotted your sample. Poke it into the gel, but keep the area small. This dyes the albumin in the blood serum. The albumin is the fastest moving component, and the dye is used to tell you how far the separation has progressed. Usually, two spots are formed use the darkest one. 

It should be noted that while the average values reported by Svensson are given in Table IV, the full data for individual runs which he reports show wide individual variations. Thus for albumin in cow serum, he obtained values as low as 34.8 and as high as 47.1%, while for guinea pig serum, the albumin values varied between 46.8 and 64.4. However, making due allowances for these variations, the data still provide clear evidence that there are great differences in the amounts of the principal electrophoretic components in the plasma of difforent species. Other electrophoretic data on a number of different animal species have recently been reported by Deutsch and Goodloe (52) and by Moore (153). 

Following an intravenous administration in rodents, positively charged complexes appear to bind serum components such as albumin in a charge density-dependent manner (40), resulting in a significant and virtually immediate increase in the size of the complexes for example, to 1 -2 pm within minutes... 

The qualitative thermodynamic explanation of the shielding effect produced by the bound neutral water-soluble polymers was summarized by Andrade et al. [2] who studied the interaction of blood with polyethylene oxide (PEO) attached to the surfaces of solids. According to their concept, one possible component of the passivity may be the low interfacial free energy (ysl) of water-soluble polymers and their gels. As estimated by Matsunaga and Ikada [3], it is 3.7 and 3.1 mJ/m2 for cellulose and polyvinylalcohol whereas 52.6 and 41.9 mJ/m2 for polyethylene and Nylon 11, respectively. Ikada et al. [4] also found that adsorption of serum albumin increases dramatically with the increase of interfacial free energy of the polymer contacting the protein solution. 

A major contribution of the free-radical scavenging activity in blood plasma is attributable to the macro-molecular proteins (Wayner et al., 1985) of which albumin is a primary component and trapping agertt (Holt et al., 1984). Serum sulphydryl levels, primarily albumin-related, are decreased in subjects with rheumatoid complicated coalworkers pneumoconiosis, indicative of exacerbated inflammatory R.OM production (Thomas and Evans, 1975). Experimental asbestos inhalation in rats leads to an adaptive but evidendy insufficient response by an increase in endogenous antioxidant enzymes (Janssen etal., 1990). Protection of the vascular endothelium against iron-mediated ROM generation and injury is afforded by the iron sequestiant protein ferritin (Balia et al., 1992). 

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