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Hemoglobin a chains

Hemoglobin A, -chain (No. 135-143) Hemoglobin A, /3-chain (No. 70-78) Hemoglobin A, a-chain (No. 117-123) Hemoglobin F, y-chain Hemoglobin A2, 5-chain Hemoglobin A, /3-chain (No. 21-21) Hemoglobin E... [Pg.195]

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 7.4. 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 7.13. Conservation of Three-Dimensional Structure. The tertiary structures of human hemoglobin ( a chain). Figure 7.13. Conservation of Three-Dimensional Structure. The tertiary structures of human hemoglobin ( a chain).
Fig. 3. Diagrammatic sketch showing the change in tertiary structure of a hemoglobin a chain on reaction with oxygen. Movement of the iron atom into the plane of the porphyrin ring causes a movement of helix F toward helix H, which expels tyrosine in position 140 from its pocket between the two helices. From (PIO), M. F. Perutz, Stereochemistry of cooperative effects in haemoglobin. Nature (London) 228, 726 (1970) with permission of the author and publisher. Fig. 3. Diagrammatic sketch showing the change in tertiary structure of a hemoglobin a chain on reaction with oxygen. Movement of the iron atom into the plane of the porphyrin ring causes a movement of helix F toward helix H, which expels tyrosine in position 140 from its pocket between the two helices. From (PIO), M. F. Perutz, Stereochemistry of cooperative effects in haemoglobin. Nature (London) 228, 726 (1970) with permission of the author and publisher.
A2. Adams, H. R., Wrightstone, R. N., Miller, A., and Huisman, T. H. J., Quantitation of hemoglobin a chains in adult and fetal goats gene duplication and the production by polypeptide chains. Ardi. Biochem. Biophys. 132, 223-236 (1969). [Pg.224]

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.]... 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.]...
Myoglobin P chain Hemoglobin a chain hemoglobin chain Hemoglobin Y chain Hemoglobin... [Pg.82]

Mekecha, T.T. Amunugama, R. McLuckey, S.A. Ion trap collision-induced dissociation of human hemoglobin a-chain cations. J. Am. Soc. Mass Spectrom. 2006,17, 923-931. [Pg.29]

Monoisotopic (mi) and average (av) peptide masses from tryptic digestion of human hemoglobin a chain [11]... [Pg.178]

Fig. 2. Five fragment masses determined from the mass spectrum of the mock unknown protein (human hemoglobin a chain) tryptic digest form the basis of peptide mapping. The mass-to-charge ratio is labeled nih on the horizontal axis. Fig. 2. Five fragment masses determined from the mass spectrum of the mock unknown protein (human hemoglobin a chain) tryptic digest form the basis of peptide mapping. The mass-to-charge ratio is labeled nih on the horizontal axis.
Chain of hemoglobin A /3-Chain of hemoglobin A Chain of myoglobin from whale... [Pg.437]

See other pages where Hemoglobin a chains is mentioned: [Pg.100]    [Pg.98]    [Pg.195]    [Pg.196]    [Pg.679]    [Pg.69]    [Pg.72]    [Pg.72]    [Pg.75]    [Pg.84]    [Pg.286]    [Pg.559]    [Pg.199]    [Pg.502]    [Pg.173]    [Pg.179]    [Pg.179]    [Pg.179]    [Pg.132]    [Pg.684]    [Pg.68]    [Pg.259]    [Pg.363]   
See also in sourсe #XX -- [ Pg.42 ]



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A chain of human hemoglobin

Hemoglobin 0 chain

Hemoglobin A

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