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Protein table

The packed columns of Shodex OHpak SB-800HQ series are packed with polyhydroxymethacrylate gels and are designed for use with high-resolution, high-speed aqueous size exclusion chromatography. The packed columns are best suited for the analysis of water-soluble polymers and proteins (Table 6.8). [Pg.193]

With a knowledge of the methodology in hand, let s review the results of amino acid composition and sequence studies on proteins. Table 5.8 lists the relative frequencies of the amino acids in various proteins. It is very unusual for a globular protein to have an amino acid composition that deviates substantially from these values. Apparently, these abundances reflect a distribution of amino acid polarities that is optimal for protein stability in an aqueous milieu. Membrane proteins have relatively more hydrophobic and fewer ionic amino acids, a condition consistent with their location. Fibrous proteins may show compositions that are atypical with respect to these norms, indicating an underlying relationship between the composition and the structure of these proteins. [Pg.142]

With increased CO2 concentrations, by the injection of CO2 gas into ponds, outputs of 3 x 104 kg dry protein per hectare per year are possible. This compares very favourable with conventional sources of protein (Table 4.3), note the low yields of meat and milk. [Pg.72]

These proteins can be subdivided into extracellular and intracellular Ca2+-binding proteins (Table 1). [Pg.291]

Ca2+-binding Proteins. Table 1 Families of Ca2+-binding proteins... [Pg.292]

Heterotrimeric G-proteins Table Appendix Receptor Proteins... [Pg.515]

S100 Proteins. Table 1 Nomenclature9 and chromosomal location of the S100 genes... [Pg.1102]

S100 Proteins. Table 2 S100 proteins in human diseases... [Pg.1105]

S100 Proteins. Table 3 S100 proteins in clinical diagnostics... [Pg.1106]

Estrogens are bound to SHBG and progestins to CBG. SHBG binds estradiol about five times less avidly than it binds testosterone or DHT, while progesterone and cortisol have little affinity for this protein (Table 42-8). In contrast, progesterone and cortisol bind with nearly equal affinity to CBG, which in turn has little avidity for estradiol and even less for testosterone, DHT, or estrone. [Pg.455]

The red blood cell must be able to squeeze through some tight spots in the microcirculation during its numerous passages around the body the sinusoids of the spleen are of special importance in this regard. For the red cell to be easily and reversibly deformable, its membrane must be both fluid and flexible it should also preserve its biconcave shape, since this facilitates gas exchange. Membrane lipids help determine membrane fluidity. Attached to the inner aspect of the membrane of the red blood cell are a number of peripheral cytoskeletal proteins (Table 52-6) that play important roles in respect to preserving shape and flexibility these will now be described. [Pg.616]

The pectinase activity was found in void volume of the washing buffer while some contaminated protein was adsorbed to the ion exchanger (Figure 1. The activity was 100% recovered. Thoug i, the enzyme was not adsorbed to the DEAE-ceUulose, but it is useful since the some contaminated proteins coidd be separated. The enzyme was approx. 10 fold purified and its specific activity increased to 48.8 unit/mg protein (Table 1). [Pg.717]

The enz3rme activity was adsorbed to the cation exchange chromatography. Three peaks of activities were found (fraction no. 78-81, 83-85 and 86-89). The major peak (no.83-85) was coUected (Figure 2. The enz3rme was purified to approx. 100 fold with the higher specific activity, 534.7 unit/mg protein (Table 1). [Pg.717]

Aromatic amine-containing haptens are converted to diazonium salts with ice-cold nitrous acid. Diazonium salts can then react with a protein at alkaline pH (around 9) through electrophilic attack of the diazonium salt at histidine, tyrosine and(or) tryptophan residues of the carrier protein (Table 7). [Pg.642]

Within each species, individual promoters resulted in distinct, tissue-dependent accumulation patterns. The cauliflower mosaic virus (CaMV) 35S promoter, for example, led to high-level accumulation in callus and leaves whereas the maize ubiqui-tin-1 promoter was the best choice for producing recombinant proteins in cereal seeds even though it is not in itself seed-specific [23]. The lack of such comparative studies for proteins other than rAbs makes it difficult to generalize an optimal expression strategy for all proteins. Tables 7.1 and 7.2 list recombinant proteins expressed in plants and provide details of the production system, promoters and other regulatory elements used in each case. [Pg.105]

Many of the initial biopharmaceuticals approved were simple replacement proteins (e.g. blood factors and human insulin). The ability to alter the amino acid sequence of a protein logically coupled to an increased understanding of the relationship between protein structure and function (Chapters 2 and 3) has facilitated the more recent introduction of several engineered therapeutic proteins (Table 1.3). Thus far, the vast majority of approved recombinant proteins have been produced in the bacterium E. coli, the yeast S. cerevisiae or in animal cell lines (most notably Chinese hamster ovary (CHO) cells or baby hamster kidney (BHK) cells. These production systems are discussed in Chapter 5. [Pg.8]

There are a surprisingly large number of evolutionarily and structurally related ion channel proteins— in the human genome more than 140 genes encode these proteins (Table 6-2) [5,38], What do they all do Experiments in progress in many laboratories are beginning to reveal the meaning of this exceptional ion channel diversity. [Pg.107]

Cholera toxin catalyzes the ADP-ribosylation of a specific arginine residue in G and Gat. This covalent modification inhibits the intrinsic GTPase activity of these a subunits and thereby freezes them in their activated, or free, state (Fig. 19-1C). By this mechanism, cholera toxin stimulates adenylyl cyclase activity and photoreceptor transduction mechanisms. The ability of cholera toxin to ADP-ribosylate G may require the presence of a distinct protein, ADP-ribosylation factor (ARF). ARF, which is itself a small G protein (Table 19-2), also is ADP-ribosylated by cholera toxin. ARF is implicated in controlling membrane vesicle trafficking (see Ch. 9). [Pg.343]

The molecules that transduce noxious heat or cold are members of the transient receptor potential (TRP) receptor family. TRP proteins (Table 57-2) form tetra-meric nonselective cation channels within the plasma membrane, allowing sodium and calcium ion influx [4]. The TRPV3 channel is activated at temperatures between 31 and39°C, TRPV1 at43°C, and TRPV2 at 52-55°C. The heat pain threshold in humans is 43°C, suggesting that... [Pg.929]

LBM can be assessed by measuring serum visceral proteins (Table 57-4). They are best for assessing uncomplicated semistarvation and recovery, and poor for assessing status during acute stress. Visceral proteins must be interpreted relative to overall clinical status because they are affected by factors other than nutrition. [Pg.662]

Table 1.7 Activity of lactate dehydrogenase after freezing and thawing in the presence of dissolved substances, which are mostly repelled by proteins (Table III from [1.18]). Table 1.7 Activity of lactate dehydrogenase after freezing and thawing in the presence of dissolved substances, which are mostly repelled by proteins (Table III from [1.18]).
The substitution of the seed flours for cowpeas or wheat flour increased the percentage protein (Table IV) in all food products and increased the chemical scores of the limiting amino acids, methionine and cystine, for all foods. [Pg.70]

Feeding studies with the rat as the test animal verified the high nutritional quality indicated by the amino acid pattern (45). Using isolates and concentrates prepared from Jewel and Centennial cultivars, PER values were equal to that of casein (milk protein) (Table IV). Examination of the amino acid patterns of sweet potato protein and casein revealed that both contained... [Pg.245]

The ras superfamily of proteins in mammalian cells is divided into three subgroups, depending upon the degree of homology between the proteins (Table 6.1) ... [Pg.195]


See other pages where Protein table is mentioned: [Pg.139]    [Pg.69]    [Pg.126]    [Pg.200]    [Pg.415]    [Pg.466]    [Pg.354]    [Pg.471]    [Pg.337]    [Pg.370]    [Pg.72]    [Pg.50]    [Pg.224]    [Pg.266]    [Pg.90]    [Pg.44]    [Pg.144]    [Pg.215]    [Pg.237]    [Pg.244]    [Pg.148]    [Pg.57]    [Pg.70]    [Pg.79]    [Pg.98]    [Pg.99]   
See also in sourсe #XX -- [ Pg.1155 ]




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