Purification of Chicken 7.1S Immunoglobulin.--Whole chicken serum was dialyzed against 0.015 ,~ Tris-HC1 pH 8.0, containing 1 ~s urea. The dialyzed serum (80 ml) was applied to a 4.5 cm X 50 cm DEAE(diethylaminoethyl)-cellulose column (DE-32 microgranular, Whatman) equilibrated with the same solvent. Elution was accomplished with a linear NaC1 grad-
IgD was detected on the surface of peripheral blood lymphocytes of five non-human primate species by direct immunofluorescence. The percentages of lymphocytes with surface IgD or IgM were comparable to the percentages reported for humans. The presence of IgD on the surface of rhesus monkey lymphocytes was confirmed by SDS-polyacrylamide gel electrophoresis of immunoprecipitated 125I cell surface protein. Reduced surface IgD was resolved into a light chain component and a heavy chain component whose mobility was identical to that of μ-chain under the conditions used.
The heavy (H) chains of three anti-streptococcal group A carbohydrate antibodies (anti-SACHO) of restricted heterogeneity, elicited in inbred Sprague-Dawley rats, were subjected to 40 cycles of automated Edman degradation. All three antibody H-chain preparations had an identical amino acid sequence and were classified as a variant of the VHIII subgroup of immunoglobulin H chains. A comparison of the H-chain sequence of these antibodies with that of pooled rat gamma chains suggests that a very minor population of H chains (closely related to the VHIII subgroup) has been 'recruited' as a consequence of this immunization. This observation further supports the notion that 'framework' and 'specificity' or 'hypervariable regions' are closely linked.
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