Human myoglobin

Varadarajan R, Lambright DG, Boxer SG (1989) Electrostatic interactions in wild-type mutant recombinant human myoglobins. Biochemistry 28 3771-3781... 

Nicolis S, Pennati A, Perani E et al (2006) Easy oxidation and nitration of human myoglobin by nitrite and hydrogen peroxide. Chem Eur J 12 749-757... 

Figure 5. Correlation of calculated and experimental values ofiV xfor ET in Ru(NH3)5(HisX)-modified human myoglobin. Key triangles, multiple-path TP calculation and circlesy EH calculation.

Figure 7.4. Amino Acid Sequences of Human Hemoglobin (a chain) and Human Myoglobin. Hemoglobin a is composed of 141 amino acids myoglobin consists of 153 amino acids. (One-letter abbreviations designating amino acids are used see Table 3,2.)...

Figure 7.12. Alignment of Human Myoglobin and Lupine Leghemoglobin. The use of the Blosum-62 substitution matrix yields the alignment shown between human myoglobin and lupine leghemoglobin, illustrating identities (orange) and conservative substitutions (yellow). These sequences are 23% identical.

Immobilization of anti-human myoglobin on CM5 chip BlocKing... 

Fig. 2 Sensorgrams of CM5/anti-human myoglobin IgG/HSA myoglobin system. (A) Covalent immobilization of IgG to flow cells. A sensorgram reading of 15,000 RU is indicated corresponding to an antibody binding capacity of - 200 finol myoglobin. (B) Myoglobin retained by flow cells 2 (FC2), and 3 (FC3). Retention of 20 fmol, and 10 fmol, of myoglobin is indicated for flow cells 2, and 3, respectively.

Fig. 3 BIA/MS of CM5/anti-human myoglobin IgG/HSA myoglobin system flow cells 2 (FC2) and 3 (FC3). Ion signals are observed in both spectra for the singly- and doubly-charged myoglobin. Retention of species other than the myoglobin is observed in flow cell 3 (marked by ), possibly due to non-specific interactions or the specific retention of myoglobin fragments.

The use of tryptic peptides derived from related proteins, e.g., horse myoglobin in the analysis of human myoglobin, as IS in targeted quantitative analysis has been proposed as well [116]. 

Figure 6.11 Alignment of identities only versus the Blosum 62 matrix. Repeated shuffling and scoring reveal the significance of sequence alignment for human myoglobin versus lupine leghemoglobin with the use of either (A) the simple, identity-based scoring system or (B) the Blosum-62 matrix. The scores for the alignment of the authentic sequences are shown in red. The Blosum matrix provides greater statistical power.

Figure 6.14 Conservation of three-dimensional structure. The tertiary structures of human hemoglobin (a chain), human myoglobin, and lupine leghemoglobin are conserved. Each herne group contains an iron atom to which oxygen binds. [Drawn from lHBB.pdb, IMBD.pdb, and IGDJ.pdb.]...

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