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Gene Review

MB  -  myoglobin

Gallus gallus

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Disease relevance of MB


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


Anatomical context of MB


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


  1. Myocardial myoglobin deficiency in various animal models of congestive heart failure. O'Brien, P.J., O'Grady, M., McCutcheon, L.J., Shen, H., Nowack, L., Horne, R.D., Mirsalimi, S.M., Julian, R.J., Grima, E.A., Moe, G.W. J. Mol. Cell. Cardiol. (1992) [Pubmed]
  2. Hemoglobin and myoglobin content in muscles of broiler chickens. Kranen, R.W., van Kuppevelt, T.H., Goedhart, H.A., Veerkamp, C.H., Lambooy, E., Veerkamp, J.H. Poult. Sci. (1999) [Pubmed]
  3. Entrapping intermediates of thermal aggregation in alpha-helical proteins with low concentration of guanidine hydrochloride. Dong, A., Randolph, T.W., Carpenter, J.F. J. Biol. Chem. (2000) [Pubmed]
  4. Rearrangement of lipid ordered phases upon protein adsorption due to multiple site binding. Yim, H., Kent, M.S., Sasaki, D.Y., Polizzotti, B.D., Kiick, K.L., Majewski, J., Satija, S. Phys. Rev. Lett. (2006) [Pubmed]
  5. Developmental change of protein constituents in chicken gizzards. Hirai, S., Hirabayashi, T. Dev. Biol. (1983) [Pubmed]
  6. Effect of zwitterionic surfactants on the separation of proteins by capillary electrophoresis. Gong, B.Y., Ho, J.W. Electrophoresis (1997) [Pubmed]
  7. Delay of onset of oviposition in pullets promoted by 6-methoxybenzoxazolinone. Brake, J.D., McNaughton, J.L., Nachman, R.J. Poult. Sci. (1985) [Pubmed]
  8. Stability properties of oxymyoglobin from chicken gizzard smooth muscle. Matsuoka, A., Iwaasa, H., Takiguchi, K., Arakawa, N., Li, L., Takagi, T., Shikama, K. Comp. Biochem. Physiol., B (1987) [Pubmed]
  9. Oxygen transport and the function of myoglobin. Theoretical model and experiments in chicken gizzard smooth muscle. de Koning, J., Hoofd, L.J., Kreuzer, F. Pflugers Arch. (1981) [Pubmed]
  10. Antibody response to myoglobins: effect of host species. Cooper, H.M., East, I.J., Todd, P.E., Leach, S.J. Mol. Immunol. (1984) [Pubmed]
  11. Involvement of the oxygen storage protein myoglobin in muscle damage under oxidative stress. Kamin-Belsky, N., Tomashov, R., Arav, R., Shaklai, N. Adv. Exp. Med. Biol. (1998) [Pubmed]
  12. Changes in myoglobin content during development and growth of chicken. Nishida, J. Nippon Juigaku Zasshi (1976) [Pubmed]
  13. Myoglobin and cytochrome oxidase in the myocardium of the developing chick. Mészáros, K., Chance, B., Holtzer, H. J. Mol. Cell. Cardiol. (1980) [Pubmed]
  14. Identical myoglobin is present in both skeletal and smooth muscles of chicken. Enoki, Y., Ohga, Y., Kawase, M., Nakatani, A. Biochim. Biophys. Acta (1984) [Pubmed]
  15. Heterogeneity in the myoglobin content of chicken heart Purkinje fibers. Kaiho, M., Anzai, M., Mukaida, M., Ishiyama, I. Histochemistry (1986) [Pubmed]
  16. Protein selectivity in immobilized metal affinity chromatography based on the surface accessibility of aspartic and glutamic acid residues. Zachariou, M., Hearn, M.T. J. Protein Chem. (1995) [Pubmed]
  17. Relationship between the concentration of myoglobin and parvalbumin in various types of muscle tissues from chickens. Nishida, J., Nishida, T. Br. Poult. Sci. (1985) [Pubmed]
  18. Precise determination of protein antigenic structures has unravelled the molecular immune recognition of proteins and provided a prototype for synthetic mimicking of other protein binding sites. Atassi, M.Z. Mol. Cell. Biochem. (1980) [Pubmed]
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