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Di-, tri-, and tetrapeptide sequences in haptoglobin. Contribution to understanding of haptoglobin structure
Amino acid sequences of haptoglobin and 11 proteins related and unrelated to haptoglobin were resolved into overlapping di-, tri-, and tetrapeptides. Comparison of the obtained peptides confirmed the existence of homology between haptoglobin and the family of serine proteases. The homology with light chain of immunoglobulins was relatively weak. A surprising similarity with concanavalin A was found. Tetrapeptide beta-turns (chain reversals), characterized by Chou & Fasman (1977, J. Mol. Biol., 115, 135-175) were compared with similar structures in light (alpha) and heavy (beta) subunits of haptoglobin.
Amino acid sequences of haptoglobin and 11 proteins related and unrelated to haptoglobin were resolved into overlapping di-, tri-, and tetrapeptides. Comparison of the obtained peptides confirmed the existence of homology between haptoglobin and the family of serine proteases. The homology with light chain of immunoglobulins was relatively weak. A surprising similarity with concanavalin A was found. Tetrapeptide beta-turns (chain reversals), characterized by Chou & Fasman (1977, J. Mol. Biol., 115, 135-175) were compared with similar structures in light (alpha) and heavy (beta) subunits of haptoglobin.