Primary structure of myoglobins from 31 species of birds

Application of proteomics to characterize and improve color and oxidative stability of muscle foods

“…Nevertheless, the accuracy can be increased by coupling MS with collision induced dissociation that produces a unique fragmentation pattern and speciesspecific amino acid sequences capable of differentiating proteins (Ponce-Alquicira & Taylor, 2000). In a detailed study, Enoki, Ohga, Ishidate, and Morimoto (2008) characterized the primary structure of 31 avian species and concluded that avian Mbs are different from their mammalian counterparts in amino acid sequence. The molecular masses of avian Mbs, in general, are 300-400 Da greater than those of livestock Mbs.…”

“…The molecular masses of avian Mbs, in general, are 300-400 Da greater than those of livestock Mbs. Although chicken Mb was characterized almost three decades ago utilizing Edman degradation, the primary structures of Mbs from ratites, such as ostrich, greater rhea, and emu have been determined recently (Enoki et al, 2008. Maheswarappa et al (2009) reported a homogenous electrospray ionization-mass spectrometry/mass spectrometry (ESI-MS/MS) fragmentation pattern for turkey and chicken Mbs which suggests similarity in their primary structure, and was confirmed by Joseph, Suman, Li, Beach, and Claus (2010) utilizing MALDI-TOF.…”

Expression patterns and adaptive functional diversity of vertebrate myoglobins

“…Most mammalian and bird Mbs have P 50 values (the O 2 tension, PO 2 , at 50% saturation) close to 1 Torr at 25°C [66][67][68] (Table 2), whereas P 50 in fish varies between~1 (e.g. bluefin tuna, blue marlin, common carp) and~4.9 Torr (rainbow trout) at 25°C [69][70][71] (Table 2).…”

Mass spectrometric characterization and thermostability of turkey myoglobin

“…In addition, our results demonstrated that the molecular mass of turkey myoglobin was 300-350 Da greater than those of other well-characterized red meat myoglobins such as pig, sheep, water buffalo, horse, yak, and red deer (Table 1), which ranged from 16,911 to 17,023 Da. However, the observed molecular mass of turkey Mb was similar to that of other avian myoglobins, such as chicken (17,291 Da; Deconinck et al, 1975), spot-billed duck (17,266 Da;Miyazaki, Uchida, & Tsugita, 1998), emperor penguin (17,471 Da;Tamburrini, Romano, Giardina, & di Prisco, 1999), and ostrich (17,297 Da;Enoki, Ohga, Ishidate, & Morimoto, 2008).…”