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High amino acids

Cloning of the rat pi opioid receptor was somewhat easier than the cloning of the <5 receptor since it was based on the knowledge of what the 3 receptor sequence was and on the assumption that 3 and pi receptors had high amino acid sequence similarity. Chen et al. [18] used probes directed against conserved regions of the 6 receptor to screen a rat brain cDNA library. cDNAs identified by this approach were cloned into expression vectors, transfected into COS cells and pi receptor expression detected with radioactive pi receptor selective ligands. [Pg.463]

The k receptor was cloned by a completely different approach. Yasuda et al. [9] employed probes against conserved regions of somatostatin receptors to screen a mouse brain cDNA library. Mouse k and 3 receptor cDNAs were isolated using this procedure that established that opiate and somatostatin receptors have high amino acid sequence similarity, consistent with their ability to bind some common ligands, such as Sandostatin. [Pg.463]

Saliva High Amino acids and mucin Minimal Hydrophilic and hydrophobic components... [Pg.331]

The ligand binding or catalytic sites are the most relevant parts of a protein domain for the development of small molecules as modulators of protein function. There is evidence that proteins with conserved folds often also have their functional sites on the same topological location. In some cases a remarkable conservatism in functional sites can be observed. This is true for the example described later in this review on similarity of Cdc25A phosphatase, acetylcholinesterase (AChE) and 1 Ifl-hydroxysteroid dehydrogenases (1 l HSD) (Fig. 9). Nevertheless, it should be stressed that the correlation patterns of amino acid sequence, protein fold and protein function remain a matter of debate. Moreover, a vast number of specific functions can be carried out by the limited number of protein domains due to the high amino acid diversity of proteins with similar folds. " ... [Pg.70]

GSK-3 is highly conserved between different eukaryotic species, displaying close DNA sequence homology. Similarly, high amino acid sequence homology indicates that GSK-3 has conserved structure and fimction in different species. GSK-3 exists in two isoforms encoded by different genes in mammals, GSK-3a and GSK-3P [1]. Both isoforms display a ubiquitous tissue expression pattern [2], but although structurally similar, they are not fimctionally redim-dant. The differential expression of GSK-3a and GSK-3P indicates that they may display different roles in cellular functions and tissues. [Pg.138]

Smartamine is a multiparticulate reservoir system consisting of amino-acid cores surrounded by a pH-sensitive coating (Fig. 2). In the present case, the principal advantage of a reservoir system is to allow high amino-acid contents. [Pg.471]

Cytochrome c oxidase is a highly conserved enzyme the three core subunits (I, II and III) encoded by the mitochondrial genome in eukaryotes has high amino acid sequence homology with prokaryotic and eukaryotic species. Detailed analysis of evolutionary conservation of lipid-binding sites in cytochrome c oxidase (Qin et al., 2007) shows that lipid binding sites are specific and... [Pg.222]

Oxidation in proteins and peptides are highly amino acid specific. The amino acid residues that are susceptible to oxidation generally fall into two groups, viz. those containing a sulphur atom (methionine, cysteine) and those with an aromatic side chain (histidine, tryptophan and tyrosine) [49]. [Pg.382]

Kato et al. [193] observed that, at low concentrations of glycine, fructose browned faster than glucose, whereas, at high amino acid concentration, the reverse occurred. However, Martins and van Boekel [194] pointed out that the rate of browning and the rate constant of the step in the reaction network that results in color formation, are two different things. They showed that increasing the initial reactant concentrations should not influence the reaction rate constants since, for the reaction of sugar (S) with the amino add (A), it follows that... [Pg.363]


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