Base protein

The hide proteins differ in amino acid composition and physical stmcture. The principal amino acids (qv) of the hide proteins are hsted in Table 1. Of particular importance is the difference in the water solubiUty of the proteins. AH of the proteins are soluble in water when heated, and upon the addition of either strong acids or bases. Proteins (qv) are amphoteric, possessing both acid and base binding capacity. 

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). 

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Shimada J, Ishchenko AV, Shakhnovich El. Analysis of knowledge-based protein-ligand potentials using a self-consistent method. Protein Sci 2000 9 765-75. 

Phillips, S. M., Tang, J. E., and Moore, D. R. (2009). The role of milk- and soy-based protein in support of muscle protein synthesis and muscle protein accretion in young and elderly persons. /. Am. Coll. Nutr. 28, 343-354. 

Wu, D., Onwulata, C., Ren, Z., Pae, M., Pang, H., and Meydani, S. (2009). Effect of dietary supplementation with a formulated nutrient mixture together with whey-based protein on immune response of young and old mice. /. Fed. Am. Soc. Exp. Biol. 23, 909.7. 

Batas, B. and Chauduri, J.B., Considerations of sample application and elution during size-exclusion chromatography-based protein refolding, /. Chromatogr. A, 864, 229, 1999. 

Dickinson, D. N. Due, M. T. L. Haskins, W. E. Gornushkin, I. Winefordner, J. D. Powell, D. H. Venkateswaran, K. Species differention of a diverse suite of Bacillus spores by mass spectrometry-based protein profiling. Appl. Environ. Microbiol. 2004,70,475 482. 

Perkins, D. N., Pappin, D. J. C., Creasy, D. M., Cottrell, J. S. (1999). Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20(18), 3551-3567. 

Widhalm et al. (1991) reported the use of noncrosslinked polyacrylamide for protein separation in fused silica capillaries. This matrix has low viscosity and can be replaced between separations, greatly facilitating automation of the separation. A wide range of noncrosslinked polymers has been used for size-based protein separations. Noncrosslinked polymers do not form a gel, and it is inappropriate to refer to this separation as gel electrophoresis. A number of names have been used for the method. In an effort to standardize nomenclature, IUPAC has used the term capillary sieving electrophoresis. 

Activity-based protein profiling (ABPP) is a chemical proteomic strategy in which active-site-directed covalent probes are used to profile the functional states of enzymes in complex proteomes. Activity-based probes (ABPs) can distinguish active enzymes from their inactive zymogens or inhibitor-bound forms. They contain a reactive group intended to modify enzyme active sites covalently and a reporter group (typically rhodamine or biotin) that assists in detection and identification of protein targets. 

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In use these soya based products, unlike egg albumen, do not coagulate. They must be used in conjunction with egg albumen or another coagulating material if coagulation is needed. The soya-based proteins have the advantage that they have approximately twice the whipping capacity of egg albumen. The modified soya protein is used by dispersing it directly in two to three times its own weight of water. It is not necessary to pre-soak this material, unlike egg albumen. 

Figure 6.7 (a) Typical sequence of events undertaken during an (adsorption-based) protein purification... 

Campagne, F. and Weinstein, H. (1999) Schematic representation of residue-based protein context-dependent data an application to transmembrane proteins. J. Mol. Graph. Model 17,207-213. 

D. N. Perkins, et al., Probability-Based Protein Identification by Searching Sequence Databases Using Mass Spectrometry Data. Electrophoresis, 20, no. 18 (1999) 3551-3567. 

D. Fenyo and R. C. Beavis. A Method for Assessing the Statistical Significance of Mass Spectrometry-Based Protein Identifications using General Scoring Schemes. Anal. Chem., 75, no. 4 (2003) 16%-114. 

Frishman, D., and Argos, P. (1995). Knowledge-based protein secondary structure assignment. Proteins 23, 566-579. 

FRET-based protein biosensors have been developed using CPEs as the lightharvesting donors in conjugation of lock-key recognition. Streptavidin is a... 

FRET to occur, and thus no FI emission is observed. The specificity of this assay was also examined for mixed samples. The mixed lysozyme samples were prepared in fetal bovine serum (FBS), human saliva and human urine. It was found that FAM emission was still visible upon addition of each mixed sample, implying that this assay has a great potential for the detection of real biological samples. This study illuminates that introduction of specific aptamer/protein interaction as the recognition event, and utilization of FRET as the signal transduction channel, is an effective way to develop CPE-based protein sensors with good specificity. 

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