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Hemoglobin efficiency

S., and Lara, A.R. (2014) Aerobic expression of VitreoscUla hemoglobin efficiently reduces overflow metabolism in Escherichia coli. BiotechnoL /., 9 (6), 791-799. [Pg.80]

Outdated Human Blood. If clinical efficacy and safety of hemoglobin solutions can be shown, the demand for product would soon outstrip the supply of outdated human blood. About 12 million units of blood (1 unit 480 mL) are used in the United States each year, and only about 500,000 outdate. The primary use of blood is in intraoperative and emergency settings. The quantity of blood available for use in production of blood substitutes depends on safety and efficient usage of blood products as well as on the demands on blood suppHes. [Pg.167]

Under physiological conditions, transfer of Et3PAufrom hemoglobin to albumin has been observed. The transfer is direct and does not require a low-molecular weight thiol such as GSH as an intermediary and indicates that inter-protein transfer of gold can occur spontaneously. The rapid and efficient manner of establishing this equilibrium (for transauration ) could determine many ofthe effects of intracellular and extracellular chemistry of gold. [Pg.303]

Hemoglobin is another heme-containing protein, which has been shown to be active towards PAH, oxidation in presence of peroxide [420], This protein was also modified via PEG and methyl esterification to obtain a more hydrophobic protein with altered activity and substrate specificity. The modified protein had four times the catalytic efficiency than that of the unmodified protein for pyrene oxidation. Several PAHs were also oxidized including acenaphthene, anthracene, azulene, benzo(a)pyrene, fluoranthene, fluorene, and phenanthrene however, no reaction was observed with chrysene and biphenyl. Modification of hemoglobin with p-nitrophenol and p-aminophenol has also been reported [425], The modification was reported to enhance the substrate affinity up to 30 times. Additionally, the solvent concentration at which the enzyme showed maximum activity was also higher. Both the effects were attributed to the increase in hydrophobicity of the active site. [Pg.197]

Kumar, C.V. and Chaudhari A. (2001) Efficient renaturation of immobilized met-hemoglobin at the galleries of alpha-zirconium phosphonate. Chemistry of Materials, 13, 238-240. [Pg.267]

Fig. 10.12 The most efficient regions for nanotube absorption lie where water and hemoglobin have absorption minima between 700 and 900nm and around 1,100nm (Braun and Smirnov 1993 Reprinted from Weissleder, 2001. With permission from Elsevier) (See Color Plates)... [Pg.243]

Many protein molecules are composed of more than one subunit, where each subunit is a separate polypeptide chain and can form a stable folded structure by itself. The amino acid sequences can either be identical for each subunit (as in tobacco mosaic virus protein), or similar (as in the a and )3 chains of hemoglobin), or completely different (as in aspartate transcarbamylase). The assembly of many identical subunits provides a very efficient way of constructing... [Pg.241]

Nagai and Thergersen found that an alternative approach was required to achieve efficient expression of the -chain subunits of human hemoglobin in E. coli [55]. In this case, P-globin was produced as a fusion protein that possessed the sequence Ile-Glu-Gly-Arg between the 31 amino-terminal residues of X cll... [Pg.137]

It is thought that during fast movement, the pH at the gills may drop too low for efficient oxygen uptake by those hemoglobins that exhibit the Root effect. To ensure a continued oxygen supply, trout and some... [Pg.222]


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See also in sourсe #XX -- [ Pg.67 ]




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