oxymyoglobin

oxymyoglobin

 [ok″se-mi″o-glo´bin]
myoglobin charged with oxygen.

ox·y·my·o·glo·bin (MbO2),

(ok'sē-mī'ō-glō'bin),
Myoglobin in its oxygenated form, analogous in structure to oxyhemoglobin.

ox·y·my·o·glo·bin

(MbO2) (ok'sē-mī'ŏ-glō'bin)
Myoglobin in its oxygenated form, analogous in structure to oxyhemoglobin.
See also: myoglobin
Mentioned in ?
References in periodicals archive ?
Lower ultimate meat pH (as observed in LL) decreases mitochondria respiration, thereby increasing the availability of oxygen to bind to Mb, and consequently increases surface oxymyoglobin levels and R630/580 [29].
The preference for meat is decreased when oxymyoglobin (acceptable cherry red color) is converted into metmyoglobin (unacceptable brown color).
When exposed to oxygen, deoxymyoglobin is transformed into oxymyoglobin, changing the colour from purple to the bright red colour associated with freshness.
Depending on the particular type of meat and its processing, the deoxymyoglobin oxygenates into oxymyoglobin at a higher concentration of oxygen.
Primary products of lipid oxidation generate changes in myoglobin such as the oxidation of oxymyoglobin (OMB) to metmyoglobin (MMB) inducing color changes [1, 7]; these changes result in a decrease in heme redox stability, rather than the oxidation of specific amino acid residues.
The differences around 432 nm were probably due to the absorption by met Hb and/or met Mb, the peak at 550 nm may be mainly caused by deoxymyoglobin, the differences around 574 nm are caused by the content of oxymyoglobin changing during different storage times [26], and the peak around 621 nm may be caused by hemin chloride [27].
However, vacuum-packaged fresh meat is unsuitable for the retail market because the lack of oxygen in the package causes a change of meat color from red to purple due to the conversion of oxymyoglobin to deoxymyoglobin [8].
NIRS technique is based on two fundamental characteristics [23,24]: relative transparency of human tissue to light in the near-infrared region (700-1000 nm) and the oxygenation-dependent absorption of oxyhemoglobin and oxymyoglobin (HbO2, MbO2) and deoxyhemoglobin and deoxymyoglobin (Hb, Mb).
Masuda, "Effective conversion of metmyoglobin to oxymyoglobin by cysteine-substituted polyphenols," Journal of Agricultural and Food Chemistry, vol.
The oxymyoglobin structure reveals its role as a muscular store of [O.sub.2] (3); additionally, this protein functions as a scavenger of reactive species of [O.sub.2] and nitric oxide (4).
[alpha] -Tocopherol slows the conversion of oxymyoglobin to metmyoglobin in beef thereby slowing the development of an undesirable brown color in displayed beef (LANARI et al., 1994).