Added Protein

In order to extend or improve the water holding capacity of processed meat, the product may 

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Some breads contain flour made from soybeans, which gives them added protein and a different texture. Soy flour absorbs water to make a gel, making the bread denser. 

E° and E2° values of +76 and +21 mV, respectively, have been measured for Hox from M. trichosporium OB3b by similar methods (63). These values are more closely spaced and imply that Hmv from this organism is thermodynamically less stable with respect to disproportionation. Addition of protein B lowered the potentials to -52 mV and -115 mV, respectively. The regulation of electron transfer to the hydroxylase with protein B and reductase observed with the M. capsulatus (Bath) MMO was not seen with this system. Instead, it was reported that the potentials of Hox and of Hox with added protein B are shifted slightly to more positive values in the presence of reductase (Table II), and the reduction was not substrate-dependent. 

Support Adsorbed Protein [mg] Ads Protein / Support [mg/g] Adsorbed Protein [%]... 

These products are made by adding protein to flour. While whey protein, soya protein, casein and yeast can be used the protein normally employed is pure vital wheat gluten. 

Diafiltration is a process whereby an ultrafiltration system is utilized to reduce or eliminate low molecular mass molecules from a solution and is sometimes employed as part of biopharmaceuti-cal downstream processing. In practice, this normally entails the removal of, for example, salts, ethanol and other solvents, buffer components, amino acids, peptides, added protein stabilizers or other molecules from a protein solution. Diafiltration is generally preceded by an ultrafiltration step to reduce process volumes initially. The actual diafiltration process is identical to that of ultrafiltration, except for the fact that the level of reservoir is maintained at a constant volume. This is achieved by the continual addition of solvent lacking the low molecular mass molecules that are to be removed. By recycling the concentrated material and adding sufficient fresh solvent to the system such that five times the original volume has emerged from the system as permeate, over 99... 

Complete removal of procyanidin is not necessary to overcome anti-nutritional effects. Removal of most procyanidin or addition of sufficient protein will overcome anti-nutritional effects of procyanidins. Small concentrations of procyanidin can be easily overcome by adding protein. 

Altered thermodynamic activity of proteins in solution arises when unreactive (or inert) macromolecules are added to a solution and occupy more than a few percent of total solution volume. Terms such as unreactive , "background, or inert are used to emphasize that the added protein need not exhibit and direct binding interaction with the protein of interest. Instead, the consequences have more to do with molecular crowding, and approximate theoretical models show that this effect depends on the shapes and sizes of the macromolecules. Thus, biological fluids are anything but ideal or dilute solutions. 

In contrast. Figure 2 shows that the percentage of protein in solution for soy isolates remains constant as the amount of added protein is increased (1 ). In other words, the amount of protein in solution increases linearly with increasing amounts of added protein. This behavior is observed for all the isolates we have studied up to the highest concentration of 18 percent. Thus, soy isolates behave as if they are composed of a completely soluble fraction (A) and a completely insoluble fraction (B). Upon the addition of solvent, the soluble fraction (A) dissolves completely while the insoluble fraction (B) remains unchanged. There is no equilibrium established between A and B such that, if B is separated from A and reslurried in additional amounts of solvent, no additional protein will go into solution. (More precisely, no evidence of microscopic reversibility was found on the time scale of the experiment,... 

This method was adapted as follows for use with the Spekker micro-cells. The volume of each component of the incubation mixture was reduced to0.1 ml. after incubation for 1 hr., 0.5 ml. of Folin-Ciocalteu reagent, diluted as above, was added. Protein was sedimented, and 0.5 ml. of the supernatant liquor was mixed with 0.5 ml. of 1.33 N sodium carbonate solution. The color was developed as before. 

The three proteins show intrinsic fluorescence due to the presence of Trp residues. Thus, although binding occurs between LCA and LTF or STF, we cannot use fluorescence of Trp residues of LCA to follow this interaction, since there will bean overlapping with the fluorescence of Trp residues of LTF or STF. Therefore, it is necessary to use an extrinsic probe, which is bound to one protein only. A covalently bound fluorophore such as fluorescein is very suitable to perform binding experiments, since there will be no real binding between the fluorophore and the added protein, c Figure 13.6 shows the fluorescence intensity at 515 nm of fluorescein bound to LCA in the presence of increasing concentrations of LTF or STF. 

Precipitate the immune complexes (antibody-antigen) by adding Protein A or G beads to the mixture, incubate, and then centrifuge the mixture. The protein A or G will bind to the Fc region of the antibodies. The beads (e.g., sepharose) associated with the Protein A/G will provide sufficient mass to the complex to allow its precipitation during centrifugation. 

The primary reaction occurring with gelatin is a complex formation between polyphenols in the wine and the protein of gelatine to give the desired floccular precipitate. The second reaction, less well understood but equally important, is the complex formation between the natural wine proteins and the added protein, i.e. gelatin. 

Culture medium, RPMI 1640 left, with no added protein and right, with 20% fetal... 

The adsorption process, unlike antigen-antibody interactions, is nonspecific. Thus, during the incubation of the immobilized antigen or antibody with enzyme-labeled antigen or antibody, the latter binds specifically to the immobilized immune reactant, but may also be adsorbed directly onto the solid phase. This nonspecific adsorption of enzyme activity can be minimized by inclusion of a nonionic detergent such as Triton X-lOO or Tween 20. These do not interfere with the antigen-antibody reaction but prevent formation of new hydrophobic interactions between added proteins and the solid phase without disrupting to any appreciable extent the hydrophobic bonds already formed between the previously adsorbed protein and the plastic surface. 

One of the striking applications of electroporation is incorporation of externally added protein into plasma membrane. Protein molecules with amphipathic nature can be stably entrapped in electroporated membrane when they reseal. This phenomenon called electroinsertion has been demonstrated in a number of investigations. For example, electroinsertion of transmembrane protein CD4 receptors [60] and glycophorin [61] was demonstrated, which may prove valuable in surface engineering and studies on transmembrane proteins. In addition, a number of exogenous peptides and protein enzymes have been introduced... 

Fig. 2 ICAM-1 production after topical application of gamma interferon to a human skin graft on nude mice. One dose (100 pi) of a liposomal (20mg/ml lipid) or aqueous (phosphate buffered saline) formulation was applied daily for three days. Active formulation contained 0.51 mg/ml gamma interferon. Placebo liposomal formulations contained no added protein. Significant differences (active versus placebo) are indicated by asterisks ( ). (Redrawn from data in Ref. l)...

Recently, new vector production systems have been developed that are free of replicating Ad (4). In this system, the Ad proteins E2A, VA, and E4 are expressed from a second helper construct in 293 cells, which provides El A and E1B gene products (Figure 1) (5). Furthermore, the reduction of rep production from the helper construct prevents the cytotoxicity in the packaging cells, which subsequently improves vector production (6). 

One major concern in the use of Ad recombinant vectors is the emergence of replication competent Ad vims as a result of recombination events between the viral sequences. Ad protein expression by replication-competent Ad vims, but also from the vector itself, results in the in vivo induction of a potent immune response. 

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