Partial structure of a rat IgD molecule with a deletion in the heavy chain.
The isolation, purification and characterization of the rat IR-731 monoclonal immunoglobulin is reported. The molecule is IgD-like, as appreciated from immunochemical and biochemical characteristics. H and L chains, Fab and Fc tryptic fragments have been isolated, analyzed, and partial sequence data have been obtained, including most cysteyl-containing peptides. The heavy chain contains a deletion which encompasses most of the CH2 domain and the beginning of the CH2 domain, and observation which does not reflect the intron-exon organization depicted for some murine heavy chains at the gene level. Basic structural features of the hinge region of the IgD molecule (extreme susceptibility to proteolytic enzymes, presence of basic amino acids near its COOH-terminus) have been found for the IR-731 molecule. In addition, partial sequence of the light chains points to the existence of K subgroups in the rat. Very limited amino acid changes have been identified in the K constant region, suggesting a possible--but limited--polymorphism which might be isotypic and/or allotypic in nature.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D007072:Immunoglobulin D / Q000302:isolation & purification; D007143:Immunoglobulin Heavy Chains / Q000302:isolation & purification; D007147:Immunoglobulin Light Chains / Q000302:isolation & purification; D011817:Rabbits; D051381:Rats; D014357:Trypsin
D000596:Amino Acids; D007072:Immunoglobulin D; D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D014357:Trypsin