Discoloration of dark-fleshed fish species during storage and processing was mainly due to the reaction of myoglobin, a monomeric globular heme protein contributed to the pigmentation of red meat fish, alone and with other muscle components. Metmyoglobin formation caused by the autooxidation of myoglobin was a major factor influencing the darkening of dark-fleshed fish meat during iced and froz...

Myoglobin, the heme-protein responsible for the characteristic color of striated muscle (Kendrew, 1954), was the first protein to have its three-dimensional structure unravelled (Kendrew, 1961). However, virtually nothing is known concerning its localization within the muscle cell. Myoglobin oxidizes benzidine in the presence of of hydrogen peroxide. This reaction is well known and is used in t...

Modulated supraparticle structures are used to improve sandwich and competitive fluoroimmunoassays. The improved methods are demonstrated on myoglobin, a key diagnostic protein for detection of heart damage. The resulting method uses microliter volumes with bovine serum samples doped with varying concentrations of equine myoglobin. These immunoassays use micron-diameter iron oxide particles as ...

The purpose of this study was to determine the myoglobin concentration in skeletal muscle fibers of chronic heart failure (CHF) patients and to calculate the effect of myoglobin on oxygen buffering and facilitated diffusion. Myoglobin concentration, succinate dehydrogenase (SDH) activity, and cross-sectional area of individual muscle fibers from the vastus lateralis of five control and nine CHF...

i’he low temperature (ca. 80 K) Soret-excited resonance Raman spectrum of the ‘myoglobin hydrogen-peroxide’ complex has been obtained and compared to those of Fe(H) and Fe(H) myoglobin. lhe RR spectra suggest that the iron atom in the Znyoglobin hydrogen-peroxide ’ complex is formally in the Fe(IV) state with a t& lowspin configuration. The iron-pyrrole-nitrogen (Fe-N,) and iron-imidazolenitrog...

The systemic response to decreasing oxygen levels is hypoxic vasodilation. While this mechanism has been known for more than a century, the underlying cellular events have remained incompletely understood. Nitrite signaling is critically involved in vessel relaxation under hypoxia. This can be attributed to the presence of myoglobin in the vessel wall together with other potential nitrite reduc...

[Purpose] Atrophy is a common phenomenon caused by prolonged muscle disuse associated with bed-rest, aging, and immobilization. However, changes in the expression of atrophy-related myoglobin are still poorly understood. In the present study, we examined whether or not myoglobin expression is altered in the gastrocnemius muscles of rats after seven days of cast immobilization. [Methods] We cond...

To unveil the mechanism of fast autooxidation of fish myoglobins, the effect of temperature on the structural change of tuna myoglobin was investigated. Purified myoglobin was subjected to preincubation at 5, 20, 50 and 40C. Overall helical structural decay through thermal treatment up to 95C was monitored by circular dichroism spectrometry, while the structural changes around the heme pocket w...

The knowledge of the metabolism and biological function of myoglobin remains very limited. In 1932, Theorell (1) described the crystallization of myoglobin from perfused horse heart. Rossi-Fanelli and Aragona (2) isolated this same protein from a number of domestic animals. Although the purification and crystallization of myoglobin of large mammalian species and the human (3) have been successf...

Myoglobin is a very important sarcoplasmic protein responsible for the colour of meat and meat products. This protein is degraded during post-mortem period (ageing) as well as during longer processes such as dry curing. In the present study, a total of eleven naturally generated fragments of myoglobin detected at the end of the processing of dry-cured ham have been identified for the first time...