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Bovine Thyrotropin Has a Specific Bioactivity 5- to 10 Fold That of Previous Estimates for Highly Purified Hormone^*

The Departments of Medicine, Veterans' Administration Medical Center, San Francisco, and the University of California San Francisco San Francisco, California 94121

Address requests for reprints to: B. Rapoport, Veterans' Administration Medical Center, Metabolism (111F), 4150 Clement Street, San Francisco, California 94121.

Abstract

Bovine TSH (bTSH) was subjected to reverse phase HPLC using a Synchropak RP-P C18 column. Elution was with a linear gradient of 0-50% 1-propranol in 0.1% trifluoroacetic acid. Individual fractions were assayed for TSH bioactivity by the cultured thyroid cell cAMP response assay. Optimum separation of biologically active TSH was obtained at a mobile phase pH of 5. Under these conditions, bTSH purified by conventional chromatographic techniques to 25 U/mg protein was purified further to approximately 200 U/mg protein. These data indicate that bioactivity is only present in a relatively small fraction of the molecules in a highly-purified TSH preparation. The implications of these findings are discussed. (Endocrinology 116:1379-1382,1985)

Footnotes

^* This work was supported by NIH Grant AM-19289 from the National Institutes of Health.

Received October 13, 1984.

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