• 1 January 1985
    • journal article
    • research article
    • Vol. 53  (2) , 240-242
Abstract
Infrared spectroscopic characteristics of deparaffinized tissue sections of the amyloid produced by medullary carcinoma of the thyroid confirmed the presence of .beta.-sheet and disordered conformations within the deposits. No evidence for .alpha.-helical structures was found. Amyloid produced by medullary carcinoma of the thyroid possessed secondary structural characteristics similar to amyloid of Ig origin. Infrared spectra were obtained directly from deparaffinized tissue sections, assuring that the chemical structure of amyloid in the recorded spectrum corresponds to that seen microscopically. This structure may or may not correspond to that in vivo, since fixation and dehydration may alter protein secondary structure.

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