Disease relevance of MB

• We postulated a role for myoglobin in the pathogenesis of congestive heart failure [1].
• Myoglobin is known to protect the mechanical function of the heart from hypoxia by acting as a sarcoplasmic oxygen reservoir and shuttle [1].
• Our data implicates a role for myoglobin deficiency in the pathogenesis of congestive heart failure and in the predisposition of doberman pinschers to dilated cardiomyopathy [1].
• Myocardium from poultry had remarkably decreased myoglobin compared to mammals (34 +/- 4 micrograms/g) with heart failure produced either by furazolidone or salt toxicity causing a further 50% reduction [1].
• The two main heme proteins, hemoglobin and myoglobin, are important factors determining meat quality aspects such as color and hemorrhage [2].

High impact information on MB

• In this study, the thermally induced aggregation processes of three alpha-helix proteins (myoglobin, cytochrome c, and lysozyme) in the presence and absence of 1.0 m guanidine hydrochloride (GdnHCl) were investigated by means of infrared spectroscopy [3].
• A comparison of the structural rearrangement of the lipid film upon adsorption of myoglobin and a synthetic peptide, each of which have multiple histidines, with that upon the adsorption of lysozyme, which has only one histidine, suggests that the lipid rearrangement in the former case is due to the multiplicity of binding sites [4].
• Myosin heavy chain, tropomyosin, and desmin were immunohistologically detected in 5-day-old gizzard primordia, but myoglobin was detected after 19 days of incubation [5].
• The addition of N-alkyl-N,N-dimethylammonio-1-propane sulfonate in phosphate saline buffer is important in minimizing protein-capillary wall interactions, and facilitated an efficient electrophoretic mobility of myoglobin and lysozyme [6].
• Half the pullets in each chamber received a standard layer mash and the other half received the same diet supplemented with 6-MBOA (MB) [7].

Biological context of MB

• The complete amino acid sequence of the myoglobin was also determined [8].
• Experimental flux data were obtained in two situations: a) high oxygen pressure throughout the layer of tissue providing maximum oxygen consumption and oxygen permeability, and b) anoxic conditions in part of the layer and with submaximal oxygen consumption and desaturation of myoglobin [9].
• Using both direct and competitive binding studies it is demonstrated that antibodies to beef myoglobin raised in sheep are able to distinguish between beef and sheep myoglobins although these two proteins differ by only six of the 153 amino acid residues [10].
• Involvement of the oxygen storage protein myoglobin in muscle damage under oxidative stress [11].
• Changes in myoglobin content during development and growth of chicken [12].

Anatomical context of MB

• Myoglobin and cytochrome oxidase in the myocardium of the developing chick [13].
• Oxygen transport and the function of myoglobin. Theoretical model and experiments in chicken gizzard smooth muscle [9].
• All these characteristics of the gizzard myoglobin were identical with those of the protein from the skeletal muscles [14].
• Heterogeneity in the myoglobin content of chicken heart Purkinje fibers [15].
• The objective of this study was to investigate the peroxidative effect of Mb/H2O2 on proteins in intact myofibrils (MF) [11].

Associations of MB with chemical compounds

• Measurements in the presence of functional myoglobin were compared with data obtained after abolishing the transport function of myoglobin by application of 1 kPa carbon monoxide [9].
• The interaction of different species variants of cytochrome c and myoglobin, as well as hen egg white lysozyme, with the hard Lewis metal ions Al3+, Ca2+, Fe3+, and Yb3+ and the borderline metal ion Cu2+, immobilized to iminodiacetic acid (IDA)-Sepharose CL-4B, has been investigated over the range pH 5.5-8 [16].

Other interactions of MB

• The wing and leg red muscles, which had larger amounts of myoglobin, contained smaller quantities of parvalbumin [17].
• Intensive research in the author's laboratory had culminated in the determination and synthesis of all the antigenic sites of myoglobin in 1975 and of lysozyme in 1978 [18].

Analytical, diagnostic and therapeutic context of MB

• Myocardial myoglobin deficiency in various animal models of congestive heart failure [1].
• A combination of spectrophotometric analysis of the total heme protein concentration and measurement of the myoglobin concentration, applying size exclusion chromatography, proved to be a reliable and reproducible method to determine the hemoglobin and myoglobin content in chicken muscles [2].
• The amino acid composition and peptide mapping results also concluded that identical myoglobin was present in the gizzard, skeletal and probably cardiac muscles [14].

References