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J N Buxbaum

Publications and source records attributed to J N Buxbaum.

45 records · Page 3Linked to original sources
PubMed1978

Gamma heavy chain disease in man: synthesis of a deleted gamma3 immunoglobulin by lymphoid cells in short and long term tissue culture.

Bone marrow cells were obtained from a patient with gamma heavy chain disease (HCD) whose serum contained a deleted immunoglobulin heavy chain. Incubation of the marrow cells with radioactive amino acids in short term tissue culture resulted in the synthesis of the labelled HCD protein. A permanent cell line was established from the peripheral blood of the patient. Similar labelling studies with the cell line and its cloned progeny demonstrated the synthesis of a protein identical in size and antigenicity to that synthesized by the marrow cells and found in the patient's serum. These experiments clearly demonstrated that, in this case of heavy chain disease, the deleted protein was the synthetic product of a clone of malignant lymphoid cells.

Amino Acids↗
PubMed1977

Analysis of thy-1 variants of murine lymphoma cells.

Cells obtained from a radiation-induced T-cell lymphoma of BALB/c mice, RLmale-1, were adapted to long-term tissue culture. Clones of cells were obtained in soft agar and a clonally derived population studied for the frequency of mutation in the expression of the surface antigen Thy-1.2 (OC3H) by immunoselection. The mutation rate was 1.05-1.50 X 10(-6) per cell per generation. Antigenic and structural analysis of prototype positive and negative clones demonstrated clear differences between them.

Animals↗
PubMedDate not supplied

Transthyretin Pro 36 associated with familial amyloidotic polyneuropathy in an Ashkenazic Jewish kindred.

Mutations in the serum protein transthyretin (TTR) cause amyloidosis involving the peripheral nerves, heart, and other organs. In Ashkenazic Jews, the only TTR variant described to date has been TTR Ile 33. We have studied DNA from another Ashkenazic Jewish kindred with familial amyloidotic polyneuropathy. Single-strand conformation polymorphism analysis, DNA sequencing, and restriction analysis indicated that this kindred has the TTR Pro 36 variant, previously described only in a Greek kindred.

Amyloidosis↗
PubMedDate not supplied

Department of medicine - rheumatology service rheumatic diseases study group.

Human heavy chain diseases offer an opportunity to examine the molecular events taking place in cells which produce naturally occurring structural variants of a well-studied complex protein. Extensive structural analyses have been carried out on many of these proteins and have revealed the existence of certain characteristic features. Current studies are beginning to elucidate the molecular biology underlying these structural features.

Epitopes↗