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Myoglobin response

The sacroplasmic proteins myoglobin and hemoglobin are responsible for much of the color in meat. Species vary tremendously in the amount of sacroplasmic proteins within skeletal muscle with catde, sheep, pigs, and poultry Hsted in declining order of sarcoplasmic protein content. Fat is also an important component of meat products. The amount of fat in a portion of meat varies depending on the species, anatomy, and state of nutrition of the animal. The properties of processed meat products are greatiy dependent on the properties of the fat included. Certain species, such as sheep, have a relatively higher proportion of saturated fat, whereas other species, such as poultry, have a relatively lower proportion of saturated fat. It is well known that the characteristic davors of meat from different species are in part determined by their fat composition. [Pg.32]

Figure 3.22 (a) Cyclic voltammogram of myoglobin covalently attached to a CNT forest in PBS solution under nitrogen atmosphere. The reversible redox behavior of the iron redox center is observed, (b) and (c) electrocatalytic response of Myoglobin/CNT forest electrode to oxygen and peroxide... [Pg.152]

The synthetic polymeric components as well as their combinations with proteins such as human serum albumin (HSA), bovine serum albumin (BSA), human serum albumin/a-interferon mixtures (HSA-IFNa) and myoglobin (MYO) did not give any negative response to in vitro and in vivo biocompatibility tests, such as platelet aggregation, complement activation, acute toxicity, and acute thromboembolic potential. [Pg.70]

FIGURE 3.18 Response to selected detectors as a function of retention volume for myoglobin (dissolved in PBS buffer at a pH of 6.9). The three detectors are the RI = refractive index signal, LS = lightscattering signal, and DP = differential pressure transducer (viscosity signal). (Courtesy of Viscotek, Houston, TX. With permission.)... [Pg.71]

Another important metal-containing enzyme, chlorophyll (structure 16.24), is structurally related to myoglobin and is responsible for photosynthesis, the conversion of water and carbon dioxide, with the aid of solar energy, to carbohydrates. [Pg.514]

Iron occurs in every mammalian cell and is vital for life processes. It is bound to various proteins and found in blood and tissues. The iron-porphyrin or heme proteins include hemoglobin, myoglobin and various heme enzymes, such as cytochromes and peroxidases. Also, it occurs in non heme compounds, such as ferritin, siderophilin, and hemosiderin. Hemoglobin, found in the red blood cells, is responsible for transport of oxygen to the tissue cells and constitutes about two-thirds (mass) of all iron present in the human body. An adult human may contain about 4 to 6 grams of iron. [Pg.410]

Ding, S.F., Xu, M.Q., Zhao, G.C., and Wei, X.W., Direct electrochemical response of Myoglobin using a room temperature ionic liquid, l-(2-hydroxyethyl)-3-methylimidazolium tetrafluoroborate, as supporting electrolyte, Electrochem. Commun., 9, 216-220,2007. [Pg.136]


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