Proteins common

TABLE 7.3 Selection of Calibration Proteins Commonly Used for the Calibration of Fractogel EMD BioSEC Columns ... 

They also bind small molecules and can be involved in protein-protein interactions. PAS domains in other proteins commonly function either as protein interaction sites or small molecule binding domains. Occasionally,... 

Formulation strategies for stabilization of proteins commonly include additives such as other proteins (e.g., serum albumin), amino acids, and surfactants to minimize adsorption to surfaces. Modification of protein structure to enhance stability by genetic engineering may also be feasible, as well as chemical modification such as formation of a conjugate with polyethylene glycol. 

There are three main classes of phycobiliproteins, differing in their protein structure, bilin content, and fluorescent properties. These are phycoerythrin, phycocyanin, and allo-phycocyanin (APC). There are two main forms of phycoerythrin proteins commonly in use B-phycoerythrin isolated from Porphyridium cruentum and R-phycoerythrin from Gastroclonium coulteri. There also are three main forms of pigments found in these proteins phycoerythrobilin, phycourobilin, and phycocya no bilin (Glazer, 1985). The relative content of these pigments in the phycobiliproteins determines their spectral properties. All of them,... 

Other proteins commonly crosslinked to (strept)avidin are chromogenic or fluorescent molecules, such as ferritin or phycobiliproteins (Chapter 9, Section 7). These conjugates can be used in microscopy techniques to stain and localize certain antigens or receptors in cells or tissue sections. 

Pantaloni et al. (1981) investigated the mechanism of initiation of tubulin assembly, and the role of MAPs in the stabilization of microtubules. For their work they used microtubule protein carried through two cycles of assembly/disassembly, followed by treatment with 1 M sodium chloride for 1 hour, and subsequent centrifugation to remove the 70,000-, 168,000-, and 210,000-molecular weight proteins commonly... 

Step 1 Reduce Fe3+ in transferrin to Fe2+, which is released from the protein. Commonly employed reducing agents are hydroxylamine hydrochloride (NH3OH+Cl )> thioglycolic acid, or ascorbic acid. 

The pertinent epithelia tissues of the oral cavity are the buccal and the sublingual ones. They are nonkeratinized tissues, both covered with a thin layer of mucus (Figure 1.8). The first is 500-800 pm thick, whereas the latter is 100-200 pm thick, and more vascularized than the former [121,122]. This difference in thickness may be a possible cause for the diversity in their permeabilities the sublingual is more permeable than the buccal mucosa, and the palatal mucosa is the least permeable. Permeability values of water and horseradish peroxidase (a 40-kDa heme protein commonly used as a permeation label) in the pig oral cavity are shown in Table 1.2. Blood vasculature in both epithelia of the oral cavity does not drain directly to... 

Ozaki M., Morisaki K., Idei W., Ozaki K. and Tokunaga F. (1995) A putative lipophilic stimulant carrier protein commonly found in the taste and olfactory systems. A unique member of the pheromone-binding protein superfamily. Eur. J. Biochem. 230, 298-308. 

A recently developed version of the specific-locus test detects electrophoretic protein variants at at least 21 loci.101 198 It is based on early test-system development by Mailing and Valcovic270 and Soares.1+24 A significant increase in the mutation frequency for ENU has been demonstrated with this test. 95 Two inbred strains of mice are used that differ at 10 loci whose protein products are electrophoretically demonstrable. In addition, mutations resulting in the loss of any of 11 other proteins common to the two strains can be detected. Males of either strain are exposed to the test substance, and, at the desired time after exposure, they are mated with females of the other strain. Later, all parental and Fi animals are examined for the biochemical characters of interest. 

However, some receptors are constitutively expressed in the nucleus and this type of receptor would not be amenable to a nuclear translocation assay. The activities of nuclear receptors may be dependent upon complex interactions with a number of coregulatory proteins, commonly known as coactivators or corepressors, and modifications by post-translational means. Cell type-specific expression levels of receptors and coregulators may contribute to some, but not all, of the molecular bases for gene and functional selectivity of receptor activity. Therefore selecting a cell line that expresses both the target receptor and the necessary cofactors may be required to design an appropriate assay. 

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