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Selective Effects of a New Metal-complexed Azo Dye on Proteins of the Reed-Sternberg Cell¹

Biological Sciences Group, Section of Biochemistry and Biophysics, The University of Connecticut, Storrs, Connecticut 06268

The sulfonated azo dye, palatinechtschwarz, a coordination complex of chromium, produces intense staining of the nucleoli of Reed-Sternberg cells. Chemical blocking tests and enzymatic digestions in conjunction with independent, specific methods for localization of amino acids established that the amino groups of lysine and arginine are the primary dye-binding sites. Reed-Sternberg cells are distinguished by certain attributes not shared by lymphocytes or histiocytes of lymph node tissue. They are totally unresponsive to the cytochemical test for histidine, whereas lymphocytic nucleoli and chromatin react strongly. The distinctive feature of Reed-Sternberg nucleoli is their persistent, though enfeebled, capacity for binding palatinechtschwarz despite alkylating treatments and proteolytic digestions which totally prevent dye-binding elsewhere in the tissue. This anomaly is thought to arise from an aberration of the nucleolar protein, perhaps involving methylation of a fraction of the amino acids. Observations and tests are described which support the plausibility of this postulate. A significant feature of these findings is that they represent a primordial condition since the lymph node tissue had not been vitiated by radiation or chemotherapeutic treatment of the patient prior to biopsy.

¹ This work was supported by a research grant (CA-08732) from the National Cancer Institute, USPHS.

Received 12/27/68. Accepted 4/ 1/69.