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Myoglobin isolation

The first three-dimensional structure of a protein determined was the dioxygen transporter myoglobin isolated from sperm whale in the ferric form (86, 87). A 153 amino acid globular protein, myoglobin contains eight helical regions (A to H) with a single heme b bound between helices... [Pg.415]

John Kendrew found that the x-ray diffraction pattern of crystalline myoglobin (isolated from muscles of the sperm whale) is very complex, with nearly 25,000 reflections. Computer analysis of these reflections took place in stages. The resolution improved at each stage, until in 1959 the positions of virtually all the non-hydrogen atoms in the protein had been determined. The amino acid sequence of the protein, obtained by chemical analysis, was consistent with the molecular model. The structures of thousands of proteins, many of them much more complex than myoglobin, have since been determined to a similar level of resolution. [Pg.137]

In order to study the function of oxygen binding by myoglobin and its effect on muscle function. Cole (Footnote 16) perfused an isolated muscle with hydrogen peroxide. Why did he do this ... [Pg.1016]

Basic Protocol 3 Isolation of Total Myoglobin for In Vitro Studies F3.3.6... [Pg.889]

Myoglobin stock solution of isolated (see Basic Protocol 3) commercial myoglobin (e.g., Sigma)... [Pg.913]

Meat discoloration studies typically involve a maximum of 5 days, with discoloration analy-sis being performed every day or on alternate days. The actual experimental time involved in the objective assessment of discoloration is not extensive and depends on the number of samples being analyzed. Colorimetric measurements with hand-held colorimeters are very rapid (three measurements per meat surface in < 1 min). Spectral scans of meat surfaces require 1 to 2 min. Extraction and analysis of ground meat products has the added step of homogenization and filtration prior to spectrophotometry, but relative to many laboratory procedures, this is relatively quick. Isolation and purification of preparative amounts of myoglobin requires only 2 to 3 days once appropriate preparations are made. Finally, metmyoglobin can be reduced to oxymyoglobin in 15 to 20 min. [Pg.918]

Some dimeric myoglobins have been isolated from the muscles of the sea-snail Nassa mutabilis ind from the clams Anadora broughtonii and A. senilis. These have no Bohr effect but show ooperative effects for the uptake of 02.1274... [Pg.689]

The NMR spectra for the different electronic configurations described for myoglobin were also studied for hemoglobin and for the isolated -and -chains (Shulman et al. (99)). The basic spectral features are similar to those of the corresponding myoglobins, but the size of the hyperfine shifts of the heme resonances is quite different. As an illustration the resonances at low fields of deoxymyoglobin and deoxyhemoglobin are compared in Fig. 31. [Pg.108]

Fig. 30. Effects of alkyl isocyanides (n-series) on the 600-MHz ring-current-shifted proton resonances of isolated a and p chains of Hb A, Hb A, and sperm whale myoglobin (Mb) in 0.2 M phosphate in D20 at pH 6.6 and 21°C CO, carbon monoxide MNC, methyl isocyanide ENC, ethyl isocyanide nPNC, n-propyl isocyanide nBNC, n-butyl isocyanide. [Adapted from Mims el al. (1983a)]. Fig. 30. Effects of alkyl isocyanides (n-series) on the 600-MHz ring-current-shifted proton resonances of isolated a and p chains of Hb A, Hb A, and sperm whale myoglobin (Mb) in 0.2 M phosphate in D20 at pH 6.6 and 21°C CO, carbon monoxide MNC, methyl isocyanide ENC, ethyl isocyanide nPNC, n-propyl isocyanide nBNC, n-butyl isocyanide. [Adapted from Mims el al. (1983a)].
Fig. 31. A comparison of the 1H chemical shifts for the E11 valine 72-CH3 protons of the various isonitrile complexes of isolated a chains (o) and p chains (A) of Hb A, the o ( ) and p ( ) chains as identified within an intact Hb A molecule, and sperm whale myoglobin ( ). Ligands CO, carbon monoxide M, methyl isocyanide E, ethyl isocyanide P, n-propyl isocyanide B, n-butyl isocyanide iP, isopropyl isocyanide and tB, tert-butyl isocyanide. [From Mims et al. (1983a)]. Fig. 31. A comparison of the 1H chemical shifts for the E11 valine 72-CH3 protons of the various isonitrile complexes of isolated a chains (o) and p chains (A) of Hb A, the o ( ) and p ( ) chains as identified within an intact Hb A molecule, and sperm whale myoglobin ( ). Ligands CO, carbon monoxide M, methyl isocyanide E, ethyl isocyanide P, n-propyl isocyanide B, n-butyl isocyanide iP, isopropyl isocyanide and tB, tert-butyl isocyanide. [From Mims et al. (1983a)].

See other pages where Myoglobin isolation is mentioned: [Pg.441]    [Pg.241]    [Pg.41]    [Pg.46]    [Pg.49]    [Pg.395]    [Pg.382]    [Pg.3]    [Pg.23]    [Pg.582]    [Pg.147]    [Pg.43]    [Pg.70]    [Pg.45]    [Pg.986]    [Pg.392]    [Pg.907]    [Pg.912]    [Pg.912]    [Pg.871]    [Pg.873]    [Pg.684]    [Pg.688]    [Pg.441]    [Pg.56]    [Pg.75]    [Pg.77]    [Pg.834]    [Pg.473]    [Pg.23]    [Pg.229]    [Pg.234]    [Pg.193]    [Pg.118]   
See also in sourсe #XX -- [ Pg.253 ]




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Myoglobin

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