Theoretical determination of the electronic structure and the spatial arrangement of ferrous iron in deoxygenated sperm whale myoglobin and human hemoglobin from Mössbauer experiments

1976 ◽  
Vol 64 (4) ◽  
pp. 1446-1455 ◽  
Author(s):  
H. Eicher ◽  
D. Bade ◽  
F. Parak
1994 ◽  
Vol 49 (8) ◽  
pp. 5133-5142 ◽  
Author(s):  
R. H. French ◽  
S. J. Glass ◽  
F. S. Ohuchi ◽  
Y. -N. Xu ◽  
W. Y. Ching

2009 ◽  
Vol 390 (1) ◽  
pp. 27-31 ◽  
Author(s):  
Paolo Ascenzi ◽  
Elisabetta De Marinis ◽  
Alessandra di Masi ◽  
Chiara Ciaccio ◽  
Massimo Coletta

1977 ◽  
Vol 167 (1) ◽  
pp. 275-278 ◽  
Author(s):  
A L Kazim ◽  
M Z Atassi

The complete antigenic structure of sperm-whale myoglobin was previously determined in our laboratory. By structural analogy with myoglobin, two regions in human haemoglobin were predicted to comprise antigenic sites. One region was on the alpha-chain [alpha-(15-23)] and the other on the beta-chain [beta-(16-23)]. These two regions were synthesized, purified and characterized, and their immunochemistry was studied. Each peptide was able specifically to bind considerable amounts of haemoglobin antibodies. In a set of homologous proteins, barring any drastic conformational or electrostatic inductive effects exerted by the substitutions, and allowing for obstruction due to subunit interaction, the determination of the antigenic structure of one protein may serve as a useful starting model for the others.


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