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Myoglobins molecular weight

Three different types of columns packed with gels of different pore sizes are available. Columns should be selected that are suitable for the molecular weight range of specific samples, as each type has a different exclusion limit (Fig. 6.41, page 215). Bovine serum albumin (BSA), myoglobin, and lysozyme show good peak shapes using only 100 mM of sodium phosphate buffer as an eluent. There is no need to add any salt to the eluent to reduce the ionic interaction between protein and gel. [Pg.205]

A typical electrospray spectrum of a high-molecular-weight material, i.e. that of horse heart myoglobin, is shown in Figure 4.11. Each of the ions observed arises from attachment of a different number of protons, and an equivalent number of charges, to the intact molecule. [Pg.165]

Table 4.1 Molecular weight of horse heart myoglobin calculated from four adjacent pair of ions observed in its electrospray mass spectrum... Table 4.1 Molecular weight of horse heart myoglobin calculated from four adjacent pair of ions observed in its electrospray mass spectrum...
Determine the charge state on the ion of m/z 1060.71 in the mass spectrum shown in Figure 4.11 by using the methodoiogy outlined above. From this, calculate the molecular weight of horse heart myoglobin. [Pg.167]

Example ESI on a magnetic sector instrument set to R = 20,000 allows for the flail resolution of isotopic peaks in case of medium-molecular weight proteins (Fig. 11.21). This enables the direct determination of the charge state of the ions from the spacing of the isotopic peaks, i.e., 1 1h- for the lysozyme ion due to the average spaces of Am = 0.091 u and 13h- for the myoglobin ion due to Am = 0.077 u. In this particular case, the lysozyme [M+llH]" ion serves as a mass reference for the accurate mass measurement of the unknown" [M+13H] ion. [103]... [Pg.460]

Figure 3.18 contains data on myoglobin obtained using a triple detection setup. A molecular weight of 21,100 is found with a viscosity of 0.0247 dl/g, and from this a hydrodynamic radius of 2.06 nm, which is essentially the same as the Stokes value of 2.0 nm reported for myoglobin. [Pg.70]

Myoglobin is a protein of molecular weight of about 17,000 with the protein chain containing 153 amino acid residues folded about the single heme group. This restricts access to the iron atom (by a second heme) and reduces the likelihood of formation of a hematin-like Fe(III) dimer. The micro environment is similar to that in Cytochrome c, but there is no sixth ligand (methionine) to complete the coordination sphere of the iron atom. Thus there is a site to which a dioxygen molecule may reversibly bind. [Pg.95]

Native-PAGE (UNIT B3.1) can be used to assess the purity of the myoglobin extract, which should produce a single protein band with a molecular weight of 17.8 kDa. [Pg.913]


See other pages where Myoglobins molecular weight is mentioned: [Pg.98]    [Pg.498]    [Pg.407]    [Pg.525]    [Pg.46]    [Pg.98]    [Pg.498]    [Pg.407]    [Pg.525]    [Pg.46]    [Pg.1148]    [Pg.129]    [Pg.1148]    [Pg.158]    [Pg.28]    [Pg.166]    [Pg.30]    [Pg.73]    [Pg.511]    [Pg.43]    [Pg.46]    [Pg.83]    [Pg.346]    [Pg.152]    [Pg.266]    [Pg.280]    [Pg.436]    [Pg.53]    [Pg.463]    [Pg.466]    [Pg.1155]    [Pg.330]    [Pg.876]    [Pg.1374]    [Pg.149]    [Pg.867]    [Pg.873]    [Pg.101]    [Pg.689]    [Pg.58]    [Pg.59]   
See also in sourсe #XX -- [ Pg.9 , Pg.124 ]

See also in sourсe #XX -- [ Pg.78 ]

See also in sourсe #XX -- [ Pg.7 ]




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