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Mammalian transport proteins

From a genetical point of view, Saccharomyces cerevisiae is an ideal organism which may be considered the Escherichia coli of eukaryotic cells [4,5]. This is true in particular for the study of metabolic regulation and for that of membrane transport [6]. Finally, the astonishing resemblance between many yeast proteins and certain mammalian-cell proteins has seriously broadened the scope of interest. Although a few reports have appeared on amino acid transport in some other yeasts, most investigations in this field have used strains of Saccharomyces cerevisiae. [Pg.220]

Huang, Q. Q., et al. Cloning and functional expression of a complementary DNA encoding a mammalian nucleoside transport protein. J. Biol. Chem. 1994, 269, 17757-17760. [Pg.274]

If we had asked this question a few years ago, the answer would have been at best equivocal. However, as was pointed out in an earlier chapter, since the enormous progress in the determination of the structure of membrane proteins, we can, on the basis of the X-ray structures of an increasing number of ion transport proteins, begin to advance hypotheses that have more and more likelihood to be close to reality. In the case of Na+ channels we are still pretty much in the dark. However, the successful determination of the structure of a number of K+ channels of both bacterial and mammalian origins represents a great leap forward in our understanding of how these channels function. [Pg.153]

Today, there are a wide variety of laboratory protein expression systems available, ranging from cell-free systems over bacterial and yeast cultures to eukaryotic models including the Xenopus oocytes or insect and mammalian cell cultures, some of which even form polarised epithelial-like cells layers. In Table 24.1, an overview of the most important systems, as well as their particular strength and weaknesses in the expression of transmembrane transport proteins is provided. [Pg.588]

Protein functions and interactions are infinitely varied in biological species— one of the major problems associated with complete classification of any proteome. Proteins may transport substances myoglobin and hemoglobin (discussed in Chapter 7) transport oxygen, and carbon dioxide, in mammalian blood. Proteins called enzymes catalyze necessary biochemical reactions. The active site of an enzyme contains those amino acids that come in direct contact... [Pg.43]

Many enzymes are glycoproteins, as are many receptors, transport proteins, and hormones. They form an integral part of the membranes of mammalian cells. [Pg.214]

If bound first by albumin, heme circulates until it is transferred to hemopexin (52). In vitro in the absence of hemopexin, nonspecific cellular uptake of heme by diffusion is facile (55), but as expected, the presence of hemopexin greatly slows uptake (54), since receptor-mediated uptake is necessarily slower and of lower capacity than diffusion-limited uptake. There is currently no evidence that either receptors for albumin or membrane transporters for heme, like those in prokaryotes, are present in the plasma membrane of mammalian cells, although such transport proteins may be present in the membranes of organelles. [Pg.210]

Serum transferrin is the transport protein of ferric iron ions in mammalians. [Pg.139]

An increase of intracellular adenosine levels can also be achieved by inhibition of nucleoside transport proteins. Mammalian nucleoside transport processes can be classified into two types on the basis of their thermodynamic properties. These classes are the concentrative, Na+-dependent transport processes and the equilibrative, Na+-independent processes. The corresponding transporters are called CNTs (concentrative nucleoside transporters) and ENTs (equilibrative nucleoside transporters) (Pastor-Anglada and Baldwin, 2001). [Pg.483]

The complete urea cycle as it occurs in the mammalian liver requires five enzymes Argininosuccinate synthase, arginase, and argininosuccinate lyase (which function in the cytosol), and ornithine transcarbamoylase, and carbamoyl phosphate synthase (which function in the mitochondria). Additional specific transport proteins are required for the mitochondrial uptake of L-ornithine, NH3, and HC03 and for the release of L-citrulline. [Pg.519]


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