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Myoglobin source

FIGURE 20.19 Crystal structure of sperm whale myoglobin. [Source Dickerson (1964). Reproduced by permission of Dr. Dickerson and Academic Press.]... [Pg.524]

A typical TIC chromatogram from an analysis of peptides resulting from enzymatic digest of myoglobin. The peaks represent individual peptides eluting from an LC column and being mass measured by a spectrometer coupled to it through a dynamic-FAB inlet/ion source. [Pg.84]

A sample of the protein, horse heart myoglobin, was dissolved in acidified aqueous acetonitrile (1% formic acid in HjO/CHjCN, 1 1 v/v) at a concentration of 20 pmol/1. This sample was injected into a flow of the same solvent passing at 5 pl/min into the electrospray source to give the mass spectrum of protonated molecular ions [M + nH] shown in (a). The measured ra/z values are given in the table (b), along with the number of protons (charges n) associated with each. The mean relative molecular mass (RMM) is 16,951,09 0.3 Da. Finally, the transformed spectrum, corresponding to the true relative molecular mass, is shown in (c) the observed value is close to that calculated (16,951.4), an error of only 0.002%. [Pg.292]

Quasielastic (Rayleigh) scattering of the 46.5 keV Mossbauer radiation was used to examine the liquid dynamics of glycerol [245, 246] and the harmonic vibrations of the nonhydrogen atoms in polycrystalline myoglobin [247] as a function of temperature. The y-quanta emitted by the Mossbauer source are... [Pg.309]

Whether the toxic effects are mainly due to anemic hypoxia or to the histotoxic effects of carbon monoxide on tissue metabolism is a source of controversy. Carbon monoxide will certainly bind to myoglobin and cytochromes such as cytochrome oxidase in the mitochondria and cytochrome P-450 in the endoplasmic reticulum, and the activity of both of these enzymes is decreased by carbon monoxide exposure. However, the general tissue hypoxia will also decrease the activity of these enzymes. [Pg.364]

Figure 6-11 Schematic Representation of the Heme Complex of Myoglobin. M = methyl, P = propyl, V = vinyl. Source From C.E. Bodwell and P.E. McClain, Proteins, in The Sciences of Meat Products, 2nd ed., J.E. Price and B.S. Sch-weigert, eds., 1971, W.H. Freeman Co. Figure 6-11 Schematic Representation of the Heme Complex of Myoglobin. M = methyl, P = propyl, V = vinyl. Source From C.E. Bodwell and P.E. McClain, Proteins, in The Sciences of Meat Products, 2nd ed., J.E. Price and B.S. Sch-weigert, eds., 1971, W.H. Freeman Co.
Reactive oxygen species can originate from intracellular sources, such as mitochondria and xanthine oxidase, or from extracellular sources such as neutrophils and macrophages [33-35]. Recently, it has been proposed that myoglobin, present in the myocytes, is a potential source of higher oxidants in reperfusion injury [36]. [Pg.334]

Source of Amino Acid at Position Myoglobin Required... [Pg.387]

ROOH = LOOH, a lipid alcohol is released and no initiation or branching can occur. In aprotic solvents or acid environments, however, H abstraction is delayed and the radicals remain active. When the heme is myoglobin, hemoglobin, or a heme protein where an internal proton source is not available, the reaction mechanism is more likely to be homolytic, yielding alkoxyl radicals with no radical on the porphyrin. [Pg.333]


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See also in sourсe #XX -- [ Pg.322 ]




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