Active myoglobin

Rice-Evans, C., Okunade, G. and Khan, R. (1989). The suppression of iron release from activated myoglobin by physiological electron donors and desferrioxamine. Free Rad. Res. Commun. 7, 45-54. 

Rice-Evans, C., Green, E., Paganga, G., Cooper, C. and Wri esworth, J. (1993). Oxidised low density lipoproteins induce iron release from activated myoglobin. FEBS Lett. 326, 177-182. 

The dioxygen ligand is said to be stabilized by the presence of strong (T-donors in the trans position. Such complexes are of specific interest as models of the active myoglobin center (473). Preliminary reports of a related copper(II) system have appeared (286). Studies on the effect of extraplanar Me SO coordination on phthalocyanine derivatives of cobalt (109) and iron (315-317) have been performed and show that, for example, the low-spin d iron(II) phthalocyanine complex dissolves in Me SO to give a diamagnetic blue solution which may be reacted further with donors such as imidazole, effecting replacement at the axial sites (62). 

Figure Bl.2.11. Biologically active centre in myoglobin or one of the subunits of haemoglobin. The bound CO molecule as well as the proximal and distal histidines are shown m addition to the protohaeme unit. From Rousseau D L and Friedman J M 1988 Biological Applications of Raman Spectroscopy vol 3, ed T G Spiro (New York Wiley). Reprinted by pennission of John Wiley and Sons Inc.

PSS-SG composite film was tested for sorption of heme proteins hemoglobin (Hb) and myoglobin (Mb). The peroxidaze activity of adsorbed proteins were studied and evaluated by optical and voltammetric methods. Mb-PSS-SG film on PG electrode was shown to be perspective for detection of dissolved oxygen and hydrogen peroxide by voltammetry with linear calibration in the range 2-30 p.M, and detection limit -1.5 p.M. Obtained composite films can be modified by different types of biological active compounds which is important for the development of sensitive elements of biosensors. 

GME glycine methyl ester GDM glutamic dimethyl ester EDA ethylendiamine GAM glucosamine HDA hexadecylamine BSA bovine serum albumin OVA ovalbumin CA carbonic anhydrase MYO myoglobin H alkaline hydrolysis for converting ester groups from GME or GDM into free carboxylic acid groups that were subsequently activated with EDC for further modifications. 

The myoflbers of muscle are not homogenous but can be categorized into red and white on the basis of ATPase activity ( ). Not only the functional properties but also the composition of the two fiber types varies widely. Red fibers, for example, have considerably more myoglobin and lipid than do white type fibers. 

In order to understand the potential for haem proteins to mediate the oxidative modification of LDLs, the interaction between ruptured erythrocytes (Paganga et al., 1992) and ruptured myocytes (Bourne etal., 1994) with LDL has been explored. Previous studies from this group have demonstrated that ferryl myoglobin radicals and ruptured cardiac myocytes, which generate ferryl myoglobin species on activation (Turner et al., 1990,... 

Dosing for iron should be divided equally into two to three doses daily. An empty stomach (1 hour before or 2 hours after a meal) is preferred for maximal absorption. After absorption, iron binds to transferrin in the plasma and is transported to the muscles (for myoglobin), liver (for storage), or bone marrow (for red cell production). Iron is not actively excreted from the body but is lost through other measures already described.7 Some studies suggest that iron absorption may be... 

The biochemical activity and accessibility of biomolecule-intercalated AMP clays to small molecules was retained in the hybrid nanocomposites. For example, the absorption spectrum of the intercalated Mb-AMP nanocomposite showed a characteristic soret band at 408 nm associated with the intact prosthetic heme group of the oxidised protein (Fe(III), met-myoglobin) (Figure 8.9). Treatment of Mb with sodium dithionite solution resulted in a red shift of the soret band from 408 to 427 nm, consistent with the formation of intercalated deoxy-Mb. Reversible binding of CO under argon to the deoxy-Mb-AMP lamellar nanocomposite was demonstrated by a shift in the soret band from 427 to 422 nm. Subsequent dissociation of CO from the heme centre due to competitive 02 binding shifted the soret band to 416nm on formation of intercalated oxy-Mb. 

G.C. Zhao, L. Zhang, and X.W. Wei, An unmediated H202 biosensor based on the enzyme-like activity of myoglobin on multi-walled carbon nanotubes. Anal. Biochem. 329, 160-161 2004). 

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