Proteins concentrations

The concentration of a pure protein in solution can be determined via its extinction at 280 nm, as long as the experimenter knows the extinction coefficient (rule of thumb 1 mg/ml of BSA has about 1 OD) and the solution contains no other U V-absorWg substances. Gill and Hippel (1989) calculate the extinction coefficient of a protein from its sequence. 

and Hippel, P. (1989). Calculation of Protein Extinction Coefficients from Amino Acid Sequences, Anal. Biochem. 182 319 326. 

Ultimately, the protein concentration is measured by invoking the Beer-Lambert law  

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Fig. 5. Anion-exchange separation of insulin and insulin A- and B-chains, over diethylaminoethyl (DEAF) in a 10.9 x 200 mm column having a volume of 18.7 mL. Sample volume is 0.5 mL and protein concentration ia 16.7 mAf Tris buffer at pH 7.3 is 1 mg/mL for each component ia the presence of EDTA. Eluent (also 16.7 mAf Tris buffer, pH 7.3) flow rate is 1.27 ml,/min, and protein detection is by uv absorbance at 280 nm. The straight line depicts the salt...

Milk and egg products are highly desired in pet foods since they supply the highest quaHty amino acid profiles with nearly 100% digestibiHty. Most milk protein concentrates are used for human foods, but some are available to pets (see Milk and milk products). An enormous quantity of whole eggs (qv) derived from egg graders, egg breakers, and hatchery operations are handled as dehydrated, Hquid, or frozen ingredients. 

The mmen is not functional at birth and milk is shunted to the abomasum. One to two weeks after birth, the neonate consumes soHd food if offered. A calf or lamb that is nursing tends to nibble the mother s feed. An alternative method of raising the neonate is to remove it from its mother at a very young age, <1 week. A common example of an early weaning situation is the dairy calf that is removed from the cow soon after birth so that the cow s milk supply might be devoted entirely to production. In this instance, the neonate requires complete dietary supplementation with milk replacer. Sources of milk replacer protein have traditionally included milk protein but may also include soybean proteins, fish protein concentrates, field bean proteins, pea protein concentrates, and yeast protein (4). Information on the digestibiUty of some of these protein sources is available (4). 

Table 9. Selected Processes for Leaf Protein Concentrate Production, 1993...

Whole leaf protein concentrate, 16.5% nitrogen-free extract and 7.9% soluble soHds. 

Table 11. Nutritive Value of Leaf Protein Concentrates and Other Protein Products ...

Commercial soy protein concentrates typically contain 70 to 72% cmde protein, ie, nitrogen x 6.25, dry wt basis. Soy protein isolates are prepared from desolventhed, defatted flakes. A three-stage aqueous countercurrent extraction at pH 8.5 is used to disperse proteins and dissolve water-soluble constituents. Centrifugation then removes the extracted flakes, and the protein is precipitated from the aqueous phase by acidifying with HCl at pH 4.5. 

Pish protein concentrate and soy protein concentrate have been used to prepare a low phenylalanine, high tyrosine peptide for use with phenylketonuria patients (150). The process includes pepsin hydrolysis at pH 1.5 ptonase hydrolysis at pH 6.5 to Hberate aromatic amino acids gel filtration on Sephadex G-15 to remove aromatic amino acids incubation with papain and ethyl esters of L-tyrosine and L-tryptophan, ie, plastein synthesis and ultrafiltration (qv). The plastein has a bland taste and odor and does not contain free amino acids. Yields of 69.3 and 60.9% from PPG and soy protein concentrate, respectively, have been attained. 

In general, nonconventional protein foods must be competitive with conventional plant and animal protein sources on the bases of cost delivered to the consumer, nutritional value to humans or animals, functional value in foods, sensory quality, and social and cultural acceptability. Also, requirements of regulatory agencies in different countries for freedom from toxins or toxic residues in single-cell protein products, toxic glycosides in leaf protein products, pathogenic microorganisms, heavy metals and toxins in fish protein concentrates, or inhibitory or toxic peptide components in synthetic peptides must be met before new nonconventional food or feed protein products can be marketed. 

L. Telek and H. D. Graham, eds., Eeaf Protein Concentrates, Avi Publishing Co., Westport, Coim., 1983. 

The nutrient sparing effect of antibiotics may result from reduction or elimination of bacteria competing for consumed and available nutrients. It is also recognized that certain bacteria synthesize vitamins (qv), amino acids (qv), or proteins that may be utilized by the host animal. Support of this mode of action is found in the observed nutritional interactions with subtherapeutic use of antibiotics in animal feeds. Protein concentration and digestibiHty, and amino acid composition of consumed proteins may all influence the magnitude of response to feeding antibiotics. Positive effects appear to be largest... 

Protein-Based Substitutes. Several plant and animal-based proteins have been used in processed meat products to increase yields, reduce reformulation costs, enhance specific functional properties, and decrease fat content. Examples of these protein additives are wheat flour, wheat gluten, soy flour, soy protein concentrate, soy protein isolate, textured soy protein, cottonseed flour, oat flour, com germ meal, nonfat dry milk, caseinates, whey proteins, surimi, blood plasma, and egg proteins. Most of these protein ingredients can be included in cooked sausages with a maximum level allowed up to 3.5% of the formulation, except soy protein isolate and caseinates are restricted to 2% (44). 

Fig. 31. Effect of pressure on flux in stirred batch-ceU ultrafilttation experiments. As the protein concentration in the feed solution increases, the maximum achievable flux decreases. The maximum flux can be adjusted by changing the turbulence in the cell (71). A, 0.9% saline B, 0.65% protein (1830 tpm) C, 3.9% protein (1830 rpm) D, 6.5% protein (1830 rpm) and E, 6.5% protein (880 rpm). To convert kPa to psi, multiply by 0.145.

Fig. 32. Maximum flux obtained with various protein solutions as a function of protein concentration according to equation 3. Feed flow rates, cm /min = A, 3000 B, 2000 C, 1000 and D, 500. The flux decreases exponentially as the protein concentration increases. The extrapolated protein concentration at no flux is the gel point for this type of solution (approx 28%). These results were obtained in a flow-through cell and demonstrate the...

Table 5. Whey Protein Concentrate Compositions from Different Sources ...

Table 6. Analyses of Commercial Soy Protein Concentrates and Isolates ...

Isolated soy proteins have also been used in whipped toppings. Soy-protein-based toppings have a lower protein concentration than caseinate-based toppings. Formulations ate adjusted to protein levels, and higher protein levels can result in off-flavors. Typical formulations for a Hquid frozen, prewhipped product are given in Table 18. 

The technique of immun obi otting, often referred to as western blotting, is frequendy used for a variety of appHcations where protein concentrations... 

Blotting techniques may be used in a variety and combination of electrophoretic systems which makes their use widespread and convenient when protein concentrations are minimal and agarose or polyacrylamide is the matrix choice. 

In some patients with IgA nephropathy (IgAN), intraglomerular coagulation plays a role in depositing fibrinogen (235,236). IgAN patients treated with urokinase show a marked improvement in urinary protein concentration, semm creatinine, and blood urea nitrogen levels (237). 

Factors to be considered in maldng the selection of chromatography processing steps are cost, sample volume, protein concentration and sample viscosity, degree of purity of protein product, presence of nucleic acids, pyrogens, and proteolytic enzymes. Ease with which different types of adsorbents can be washed free from adsorbed contaminants and denatured proteins must also be considered. 

Before protein molecules attain their native folded state they may expose hydrophobic patches to the solvent. Isolated purified proteins will aggregate during folding even at relatively low protein concentrations. Inside cells, where there are high concentrations of many different proteins, aggregation could therefore occur during the folding process. This is prevented by... 

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