Abstract
The partial amino acid sequence of rabbit heavy (H) chains of allotype a1, a2, and a3 was determined. The H chains were derived from restricted antipolysaccharide antibodies which were shown to be precipitated quantitatively by antiallotype sera raised against pooled immunoglobulins.
The N-terminal half of the H chains (C1 fragment) was isolated from a CNBr digest and subjected to automated Edman degradation. Extended homology with known sequences from rabbit pooled H chains indicated that C1 fragments were cleaved between residues 34 and 35 and/or 79 and 80. One additional cleavage site was observed at position 110 in two H chains.
Section 80 to 94 of a1, a2, and a3 restricted H chains showed little sequence variation. No simple correlation between the identity of a single amino acid residue and the allotype of the H chain could be determined.
