It is known, that lipid peroxidation is one of the main factors limiting the quality and acceptability of meat and other animal tissues. The current data concerning connection of heme and peroxidation were summarized and analysed here. The muscle food compounds that are most influenced by oxidative processes include unsaturated fatty acids of lipids, amino acids of proteins and heme groups of p...

Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O2 by its heme residue, a porphyrin ring:iron ion complex. Since the initial discovery of its structure over 40 years ago, wide-ranging work by many investigators has added importantly to our understanding of its function and regulation. Functionally, myoglobi...

Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O2 by its heme residue. Myoglobin is an essential oxygen-storage hemoprotein capable of facilitating oxygen transport and modulating nitric oxide homeostasis within cardiac and skeletal myocytes. Functionally, myoglobin is well accepted as an O2- storage prote...

Its prominence has long made myoglobin a substance of general interest. Distributional surveys have provided useful and suggestive correlations with repetitive types of muscle, notably cardiac, but a direct demonstration of the function of myoglobin has not been made except in the special case of oxygen storage in diving mammals. The concentration of myoglobin in muscle has been reported as inc...

The vibrational energy relaxation of dissociated carbon monoxide in the heme pocket of sperm whale myoglobin has been studied using equilibrium molecular dynamics simulation and normal mode analysis methods. Molecular dynamics trajectories of solvated myoglobin were run at 300 K for both the delta- and epsilon-tautomers of the distal histidine, His64. Vibrational population relaxation times wer...

Recombinant human myoglobin mutants with the distal His residue (E7, His64) replaced by Leu, Val, or Gln residues were prepared by site-directed mutagenesis and expression in Escherichia coli. Electronic and coordination structures of the ferric heme iron in the recombinant myoglobin proteins were examined by optical absorption, EPR, 1H NMR, magnetic circular dichroism, and x-ray spectroscopy. ...

ECENTLY much attention has been focused on the protein binding of hemoglobin. The hemoglobin binding proteins, collectively called haptoglobin, have been thoroughly studied by several workers.’5 Indentification of these substances has helped to clarify the concept of “renal threshold” for hemoglobin excretion.5’6’9 Subsequently, in an investigation of the difference in “renal threshold” of myog...

We developed surface modification tools for the fabrication of a bioelectronic device which consists of a myoglobin monolayer self-assembled on an 11-MUA layer. To utilize a single protein as the active element, it was necessary to reduce protein aggregation on the protein layer in the nanobio electronic device, which was developed in our previous study and shown to display basic biomemory func...

Since the first description by Theorell (11) of a process of isolating and purifying myoglobin from horse heart by crystallization, several workers have succeeded in preparing myoglobin by Theorell’s procedure. Roche and Vieil (8) and Rossi and Aragona (9) have described methods less arduous than Theorell’s. Their methods, however, sacrifice yield to gain simplicity. We have developed a modific...

A method is described for the assay of myoglobin in all mvoglobin containing tissues of the rat, in particular the heart and diaphragm. Total body myoglobin increased 707~ above sea level values, both in animals taken from sea level to 12,500 feet and in animals born and reared at 12,500 feet. In comparison with the muscle hemoglobin concentration increase of 500/& the blood hemoglobin concentr...