The primary sequence of the beta chain of Hb type III of the Virginia white-tailed deer (Odocoilus Virginianus), a comparison with putative sequences of the beta chains from four additional deer hemoglobins, types II, IV, V, and VIII, and relationships between intermolecular contacts, primary sequence and sickling of deer hemoglobins.

Abstract

The amino acid sequence of the βIII chain of the hemoglobin type III present in a Virginia white-tailed deer, Odocoilus Virginianus, was determined by automatic sequencing of the intact chain, of three large fragments, and of two tryptic peptides. Analyses of the β chains of type III Hb's collected from four additional animals have uncovered individually occurring silent mutations at positions 72 or 125 or 144. The more limited data on the β chain of Hb type II suggest 8 structural differences between the βII and βIII chains which are located at positions 56, 66, 69, 70, 87, 135, 143, and 144. The β chain of Hb type IV likely is a variant of the βII chain in which lysyl residue in position 87 is replaced by a glutaminyl residue. The “non-sickling” hemoglobins V and VII have closely related 6 chains which differ considerably in their structures from the β chains of “sickling” Hb types II, III and IV. Marked variation is present in the amino terminus while at least five isoleucyl residues are present in the...