Enzymes myoglobin

In liver, muscle and other tissues iron is taken up by the cells when transferrin saturation levels are high and deposited first in ferritin and subsequently transferred to haemosiderin. This pool of ferritin iron is most likely used within these cells to meet requirements for synthesis of haem enzymes, myoglobin and other non-haem iron proteins. The ferritin can also store iron released from the breakdown of such iron containing proteins in the course of their turnover. Mobilisation of iron from these tissues once again probably involves reduction of iron to Fe2+ and its transfer across the cell membrane to transferrin. In such tissues the level of transferrin saturation seems likely to play a major role in determining the balance between deposition of iron in ferritin and its mobilization from the storage form. 

Using this concept the enzyme myoglobin was successfully encapsulated by a photo-cross-linked polymer membrane and the pH-dependent activity was reported [9], This principle offers a high potential for biotechnological apphcations. Similarly, pH-sensitive swelling of the cross-linked membrane can also be used for controlled dmg release systems. 

Yu et al. have covalently linked myoglobin and horseradish peroxidase to an aligned SWCNT electrode through the amide linkage. Quasi-reversible Ee +/Ee + voltammetry was observed for the iron heme enzymes, myoglobin, and horseradish peroxidase. The results demonstrated that the trees in the nanotube forest are potent current collectors that conduct electrons from the external circuit to the redox sites of the enzymes. 

The abihty of iron to exist in two stable oxidation states, ie, the ferrous, Fe ", and ferric, Fe ", states in aqueous solutions, is important to the role of iron as a biocatalyst (79) (see Iron compounds). Although the cytochromes of the electron-transport chain contain porphyrins like hemoglobin and myoglobin, the iron ions therein are involved in oxidation—reduction reactions (78). Catalase is a tetramer containing four atoms of iron peroxidase is a monomer having one atom of iron. The iron in these enzymes also undergoes oxidation and reduction (80). 

Figure 2.10 Examples of schematic diagrams of the type pioneered by Jane Richardson. Diagram (a) illustrates the structure of myoglobin in the same orientation as the computer-drawn diagrams of Figures 2.9b-d. Diagram (b), which is adapted from J. Richardson, illustrates the structure of the enzyme triosephosphate isomerase, determined to 2.5 A resolution in the laboratory of David Phillips, Oxford University. Such diagrams can easily be obtained from databases of protein structures, such as PDB, SCOP or CATH, available on the World Wide Web.

In this form, Alhas the units of torr.) The relationship defined by Equation (A15.4) plots as a hyperbola. That is, the MbOg saturation curve resembles an enzyme substrate saturation curve. For myoglobin, a partial pressure of 1 torr for jbOg is sufficient for half-saturation (Figure A15.1). We can define as the partial pressure of Og at which 50% of the myoglobin molecules have a molecule of Og bound (that is, F= 0.5), then... 

Following massive crush injury, myoglobin released from damaged muscle fibers colors the urine dark red. Myoglobin can be detected in plasma following a myocardial infarction, but assay of serum enzymes (see Chapter 7) provides a more sensitive index of myocardial injury. 

The 4 g of iron in the human body is normally com-partmented into its functional locations in the haem- and non-haem-containing, and iron-binding proteins and enzymes (Fig. 3.5). The majority (65%) of the iron is in the divalent state in haemoglobin and myoglobin, which are involved in the transport and storage of oxygen in erythrocytes and myocytes, respectively. The remainder is distributed between storage sites, predominantly in the... 

The first four materials (IRMM/IFCC-452, 453, 454, 455) are expected to be released during 2000. Projects on the certification of reference materials for cardiac marker (myoglobin) and total protein concentration in serum are under discussion. Even so the number of available CRMs for clinical chemistry and occupational toxicology is still limited. This has to do with the complexity of physiological compounds (e.g. proteins), the instabihty (e.g. enzymes), or the volatility (e.g. solvents). 

A series of enzyme and proteins (met-myoglobin, lysozyme, met-hemoglobin, glucose oxidase, a-chymotrypsin) was also immobilized in a-ZrP by Kumar et al. [134]. Binding constant values clearly confirm the high affinity of the various proteins with the host structure (Table 15.4). 

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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