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Biomedical subjects

J J Cebra

Publications and source records attributed to J J Cebra.

At least 127 records · Page 7Linked to original sources
PubMed1971

Peyer's patches: an enriched source of precursors for IgA-producing immunocytes in the rabbit.

The proliferative and differentiative potential of Peyer's patch, peripheral blood, and popliteal lymph node cells was assessed by allogeneic cell transfer followed by quantitation of donor immunocytes by immunofluorescence. It was found that Peyer's patches are a highly enriched source of cells which have the potential to proliferate and differentiate into IgA-producing immunocytes and that the Peyer's patch cells are far more efficient in seeding the gut of irradiated recipient rabbits with donor cells that give rise to immunoglobulin-producing cells than cells from peripheral blood or popliteal lymph nodes.

Animals↗
PubMed1971

Selective simulation of allelic expression: effectf antibodies to allotypic markers on lymphoid cells.

Peripheral blood leukocytes from rabbits which were heterozygous (b(5)/b(9)) for markers on their immunoglobulin light chains were maintained in vitro for up to 24 hours in the presence or absence of antibody to b9. After culture they were transferred into lethally irradiated b(4)/b(4)hosts. Recipients of cells exposed to antibodies to allotype markers showed a striking increase in concentration of circulating b9 molecules and number of b9 plasma cells in their spleens compared pared to control animals receiving untreated cells from the same donor. There was no appreciable difyerence between the two groups of recipients with respect to their content of b5 molecules and immunocytes.

Alleles↗
PubMed1968

Common peptides from the N-terminal half of heavy chain of immunoglobulin G from normal rabbit serum and a specific antibody.

Fragment C-1, the N-terminal half of the heavy chain of rabbit immunoglobulin G, was prepared by cyanogen bromide cleavage from the heavy chain of immunoglobulin G obtained both from the pooled serum of normal rabbits and from specific anti-dinitrophenyl antibody. Tryptic digestion of fragment C-1 after the lysine residues had been allowed to react with S-ethyl trifluorothioacetate led to the isolation of six peptides from inert immunoglobulin G and specific antibody that appear to account for most of this section of the heavy chain. This approach should make possible comparative sequence studies of the Fd section of the heavy chain from different allotypes and from specific antibodies.

Amino Acids↗
PubMed1968

The partial sequence of two large peptides from the N-terminal half of heavy chains from normal rabbit immunoglobulin G.

The partial amino acid sequence of two large peptides is described. These were prepared from the N-terminal half of the heavy chain of immunoglobulin G from pooled normal rabbit serum by tryptic digestion after the in-amino groups of the lysine residues had been blocked with S-ethyl trifluorothioacetate. These peptides are believed to account for about 145 residues of fragment C-1, the N-terminal section of rabbit immunoglobulin G heavy chain prepared by cyanogen bromide cleavage. The evidence from the present paper and the preceding paper (Cebra, Givol & Porter, 1968) suggests that it may be possible to deduce a predominant amino acid sequence for most, if not all, of this section of the molecule.

Amino Acid Sequence↗