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Immunochemistry of sperm-whale myoglobin

1973; Elsevier BV; Volume: 328; Issue: 2 Linguagem: Inglês

10.1016/0005-2795(73)90262-6

1878-1454

J. Koketsu, M. Zouhair Atassi,

Monoclonal and Polyclonal Antibodies Research

Previous reports from this laboratory have shown that in the entire sequence 120–153 of myoglobin (Mb), a single antigenic reactive region existed within sequence 140–151. In the preceding communication, it was demonstrated that lysines 140 and 145 were not essential parts of a reactive region in native Mb. It was therefore concluded that the reactive region occupied the sequence 146–151. In the present paper, strong support from an independent approach is provided by studying the immunochemistry of synthetic peptides corresponding to various parts of the region. Peptides 146–151, 145–151, 146–153 and 147–153 were prepared by solid phase peptide synthesis, purified, characterized and their interaction with three different antisera to Mb studied. With antiserum G1, peptides 145–151, 146–151 and 146–153 possessed comparable inhibitory activities of the reaction of Mb with its antisera. For this antiserum, therefore, residues 145 on one side and 152 and 153 on the other added no contribution to the inhibitory ability, and the reactive region against this antiserum occupied sequence 146–151 entirely. Similarly, in antiserum G3, specificity was directed against a reactive region occupying sequence 146–151. With antiserum G4, the inhibitory abilities of peptides 146–151 and 146–153 were comparable but appreciably lower than that of peptide 145–151. For antiserum G4, lysine 145 may be part of the antigenic reactive region of the free peptide. With the present antisera, peptide 147–153 exhibited a negligible inhibitory activity. From these findings, it was concluded that the antigenic reactive region in segment 120–153 occupies sequence 146–151 invariably, + lysine 145 with some antisera.