Abstract
Extracts of transplantable rat medullary thyroid carcinomas were fractionated by concanavalin A-agarose chromatography and SDS-polyacrylamide gel electrophoresis. While tumor extracts contained mostly (greater than 90%) native calcitonin, 4 distinct larger calcitonin species (Mr = 27,000, 17,000, 13,700, and 9,600) were also observed. Glycoprotein fractions from lectin-affinity chromatography of the tumor extracts contained 0.3-1.5% of the total immunoreactive calcitonin. Gel electrophoresis of the pooled glycoprotein fractions demonstrated that the predominant forms of immunoreactive calcitonin were larger than calcitonin monomer. One high molecular weight species (Mr = 9,600), isolated in sufficient quantity from the polyacrylamide gels for reapplication to concanavalin A-agarose, was specifically eluted from the lectin, indicating that it was a glycoprotein. These results are the first evidence that intact C-cells contain at lest one high molecular weight glycoprotein form of immunoreactive calcitonin and suggest that addition and removal of carbohydrate side chains occur during processing of calcitonin precursors to the native hormone.
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