Hydrophilicity and antigenicity of proteins—A case study of myoglobin and hemoglobin.
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Date
1989-06
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Abstract
Hydrophilicity index is used to locate antigenic determinants on two related
groups of proteins—myoglobin and hemoglobin. The data on 41 species (including 34
mammals) of myoglobin show that average hydrophilicity for the complete myoglobin
molecules as well as the average hydrophilicity for all hydrophilic regions put together
seem to remain constant; the variation in the size and location of the antigenic
determinants in these species is very small indicating that the antigenic sites are not shifted
during evolution. In the case of both the proteins there is a good agreement between the
antigenic sites picked up by using hydrophilicity index and the experimentally determined
antigenic sites. The data on 56 species of hemoglobin α-chains and 44 species of hemoglobin
β-chains showed that although there are few sites on hemoglobin which have remained
invariant during evolution, there is a significant variation in other sites in terms of either a
splitting of a site, or a drastic change in the hydrophilicity values and/or a length of the
site. Comparison of the hydrophilicity data on these two groups of proteins suggests that
hemoglobins which perform a variety of functions as compared to myoglobins are evolving
faster than myoglobins supporting the contention of earlier workers.
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Keywords
Hydrophilicity, antigenic sites, myoglobin, hemoglobin, evolution.
Citation
Devi A Sharada, Rehana Tasneem, Kolaskar A S, Pandit M W. Hydrophilicity and antigenicity of proteins—A case study of myoglobin and hemoglobin. Journal of Biosciences. 1989 Jun; 14(2): 133-142.