Hemoglobin, trout

Arylhydrocarbon (benzo[a]pyrene) hydroxylase, benzphetamine-N-demethylation, ethylmorphine-N-demethylation, ethoxycoumarin-0-deethylation and ethoxyresorufin-0-deethylation were performed by published procedures (31,32,33,34), but optimized for use with trout microsomes as described previously (30, 35). Hemoprotein P-450 was determined by the procedure of Estabrook et al. (36) to avoid spectral interference by hemoglobin. Microsomal protein content was estimated either by the method of Ross and Shatz (37) or Lowry et al. (38), using bovine serum albumin standards. 

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... 

The stabihty of trout hemoglobin was examined in the presence of some organotin compounds. Tributyltin and triphenyltin chlorides protect Hbl from the oxidation the same compounds accelerate precipitation process in HbFV to a great extent. Mercury p-hydroxymercurobenzoate, an agent blocking free SH-groups of the protein, abolished the ability of triphenyltin chloride to decrease the oxidation rate of Hbl". ... 

Figure 2.11 Plot showing the influence of the presence and absence of heterotropic ligands for various hemoglobins, n, as defined in Figure 2.4, plotted as a function of the midpoint potential for 7, Hb Aq in 0.05 M MOPS, 0.2 M NaNOs, and 0.25-0.6 mM IHP (in excess over [heme] which varied from 0.1 to 0.23 mM) 2, Hb Aq in 0.05 M MOPS, 0.2 M NaNOs 5, Trout I Hb in 0.05 M MOPS, 0.2 M NaN03 4, Hb Aq in 0.2 M MOPS 5, Hb Tq in 0.05 M MOPS 6, HbCPA in 0.05 M MOPS, 0.2 M NaNOs, and 0.25-0.6mM IHP (in excess over [heme]) 7, HbCPA in 0.05 M MOPS, 0.2 M NaNOs 5, HbCPA in 0.2 M MOPS 9, hMb in 0.05 M MOPS, 0.2 M NaN03. Additional conditions Pt mesh electrode [Ru(NH3)6Cl3] = 0.30-1.1 mM [heme] = 0.1-0.23 mM pH 7 20 °C. HbCPA is carboxypep-tidase digested Hb. Figure adapted from ref 26 and used with permission.

Molecular Adaptation in Physiological Requirements The Hemoglobin System of Trout... 

Table 11.5. Relative autoxidation rates of hemoglobin from trout, chicken and beef during storage at 4°C and formation of methemoglobin ...

Richards, M.P., Modra, A.M. and Li, R. Role of deoxyhemoglobin in lipid oxidation of washed cod muscle mediated by trout, poultry and beef hemoglobins. MeatSci. 62,157-163 (2002). 

In a recent study Chiancone et al. [469] investigate the Cl binding to the two main hemoglobin components in trout blood, Hb-Trout I and Hb-Trout IV. These two hemoglobins from the species Salmo irideus are electrophoretically different and may be separated. The two components have strikingly different functional properties. A Root effect (the equivalent of the Bohr effect for human hemoglobin),... 

The Cl excess line width in the presence of the two trout hemoglobins was studied as a function of sodium chloride concentration. No significant difference between the deoxy and carbon monoxide derivatives was observed for Hb-Trout IV in the range 0.3 to 0.8 M NaCl. 

Figure 24.22 Hemoglobin. The two a subunits of hemoglobin are shown in blue and green. The two )3 subunits are shown in yellow and cyan. The four heme groups are shown in purple, and their iron atoms are in red. (PDB ID lOUU, http //www. pdb.org. Tame, J.R., Wilson, J.C., Weber, R.E. The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms. J. Mol. Biol. 259, pp. 749-760, 1996.)...

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