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In practice, gel filtration can be used to separate proteins by molecular weight at any point in a purification of a protein. It can also be used for buffer exchange - a protein dissolved in a sodium acetate buffer, pH 4. 8, can be applied to a gel filtration column that has been equilibrated with tris buffer, pH 8. 0. Using the tris buffer, pH 8. 0, as the mobile phase, the protein moves into the tris mobile phase as it travels down the column, while the much smaller sodium acetate buffer molecules are totally included in the porous beads and travels much more slowly than the protein.
On release of the deforming stresses, these molecules tend to revert to recoiling. At low shear rates, Brownian motion of the segments occurs, and, therefore, reentanglement is a faster rate than orientation. At high shear rates, the reentanglement rates were slower than the orientation rates, thus resulted in less viscous polymers , and this reasons supports the reduction of polymer viscosity at high shear rate which is several orders of magnitude smaller than the viscosity at low shear rates. Although the viscosity of the UHMWPE/HDPE blends was lower at high shear rate, the processability of UHMWPE/HDPE blends with high content of UHMWPE was reduced. These results were expected due to the high amount of UHMWPE which has high-molecular-weight.
The hydrolytic products have an α-configuration. Specifically, α-amylase catalyzes the hydrolysis of internal α-1,4-glucan links in polysaccharides containing 3 or more α-1,4-linked D-glucose units, yielding a mixture of maltose and glucose. Amylolytic activity is present in all living organisms, but the enzymes vary remarkably, even from tissue to tissue within a single species. A protein fraction from various plants, though usually prepared from beans (particularly Great Northern and red kidney beans), is capable of inhibiting the action of α-amylase in vitro. As prepared from red kidney beans, this protein fraction is a glycoprotein with a molecular weight.