Additives proteins

Protein acidulant Protein additives Protein ammo acids a-l-Proteinase inhibitor Protein-based mimetics Protein Ca [42617-41-4] Protein channels Protein chromatography Protein crystal growth... 

Metabolic Functions. The functions of the thyroid hormones and thus of iodine are control of energy transductions (121). These hormones increase oxygen consumption and basal metaboHc rate by accelerating reactions in nearly all cells of the body. A part of this effect is attributed to increase in activity of many enzymes. Additionally, protein synthesis is affected by the thyroid hormones (121,122). 

In addition protein domains have been identified which bind to modified histone tails. The so-called bromodomains bind to acetylated histone tail, but have little or no affinity to unmodified tails. Further known binding domains include chromodomains and SANT domains which possess preferential binding to methylated and unmodified tails. 

A number of additional proteins play various roles in the structure and function of muscle. They include titin (the largest protein known), nebufin, a-actinin, desmin, dystrophin, and calcineurin. Some properties of these proteins are summarized in Table 49-2. 

Protein 4.1, a globular protein, binds tightly to the tail end of spectrin, near the actin-binding site of the latter, and thus is part of a protein 4.1-spectrin-actin ternary complex. Protein 4.1 also binds to the integral proteins, glycophorins A and C, thereby attaching the ternary complex to the membrane. In addition, protein 4.1 may interact with certain membrane phospholipids, thus connecting the lipid bilayer to the cytoskeleton. 

Finally, one must take into account that in using a coupled enzyme assay one must produce, or purchase, not only the target enzyme of interest but also the coupling enzymes and any co-substrates required for these additional protein reagents. Hence a coupled enzyme assay can be quite expensive to implement, especially for large library screening. In some cases the cost may be prohibitive, precluding the use of a particular coupled enzyme assay for HTS purposes. 

Fig. 12.5. Schematic summary of the eight T. canis proteins containing predicted SXC (NC6) domains. The consensus is shown in the N-terminal domain of PEB-1 (phosphatidylethanolamine-binding protein-1) as xCxDxxxDC(6x)C(11x) RCxxTCxxC. This consensus is faithfully repeated in MUC-1 (mucin-1), MUC-2, MUC-4 and MUC-5, and in all but the C-terminal domain of MUC-3. This domain (and the C-terminal SXC domain of PEB-1) show consensus spacing but some variation in consensus residues. Two additional proteins with quadrupled SXC domains differ in spacing between cysteines-2, -3 and -4, and show more variation in consensus residues. These are VAH-1 (venom allergen homologue) and HUF-001 (homologue of unknown function-001).

TonB-dependent receptor I (kDa) Additional proteins (kDa) Substrates Organism... 

As is apparent from Fig. 14.6, two additional protein bands with apparent molecular weights of 48 and 38 kDa were seen in sample 2 but were absent in sample 1. Moreover, the intensity for both bands was significantly reduced in sample 3, suggesting that they were retained on the streptavidin-agarose due to specific binding to PatA. 

We found that solutions of hen egg white lysozyme, bovine ribonuclease A (RNase A), or a 1 2 mol ratio of bovine carbonic anhydrase lysozyme formed opaque gels within 2 min when mixed with an equal volume of 20% NBF.25,26 Multi-protein tissue surrogates comprised of 50% w/v lysozyme and up to four additional proteins have also been formed (Fowler et al., unpublished results). After overnight fixation, the surrogates were firm and sliced easily with a razor blade for sampling. To determine the optimal... 

The tissue surrogates described here clearly represent a simplification of real FFPE tissues. However, they represent a useful and efficient construct for the evaluation and optimization of tissue extraction conditions for proteomic studies. More informative studies will likely be realized by using more complex tissue surrogates, which can be created by incorporating additional proteins into lysozyme solutions. Tissue surrogates comprised of up to five proteins have been successfully analyzed by MS (Fowler, unpublished data). Additionally, RNA, DNA, lipids, or carbohydrates can be added at nanomolar to millimolar concentrations to increase the complexity of the model system to better mimic whole tissue. The use of these more complex tissue surrogates should facilitate the development of protein recovery protocols optimal for proteomic investigation. 

Additional protein constituents of the intrinsic cascade include prekallikrein, an 88 kDa protein zymogen of the protease kallikrein, and high molecular mass kininogen, a 150 kDa plasma glycoprotein that serves as an accessory factor. 

These findings have raised questions of which additional proteins are the molecular targets of FTase inhibitors. One class of candidates involves members... 

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