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A monoclonal antibody directed against bovine TSH was obtained by hybridoma technology. This antibody was specific for TSH and did not react with bovine LH and FSH. Affinity chromatography of crude TSH was performed on anti-TSH Sepharose. Bovine TSH was purified in a single step to near homogeneity by this technique, as shown by cation exchange chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified TSH. The biological activity of the hormone was not affected during the purification, as determined by [3H]thymidine incorporation of the TSH-dependent FRTL5 cell line. The results indicate that affinity purification of TSH by means of a monoclonal antibody is a simple one-step procedure for the production of biologically active, highly purified TSH.
A J Lock, and
J van Denderen, and
L A Aarden
November 1981,
Comptes rendus des seances de l'Academie des sciences. Serie III, Sciences de la vie,
A J Lock, and
J van Denderen, and
L A Aarden
December 2002,
The Journal of clinical investigation,
A J Lock, and
J van Denderen, and
L A Aarden
July 1969,
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
A J Lock, and
J van Denderen, and
L A Aarden
January 2003,
Hormone research,
A J Lock, and
J van Denderen, and
L A Aarden
January 1967,
Endocrinology,
A J Lock, and
J van Denderen, and
L A Aarden
August 1990,
The Indian journal of medical research,
A J Lock, and
J van Denderen, and
L A Aarden
May 1994,
The Journal of allergy and clinical immunology,
A J Lock, and
J van Denderen, and
L A Aarden
February 1985,
Biochemical and biophysical research communications,
A J Lock, and
J van Denderen, and
L A Aarden
January 1982,
Endocrinology,
A J Lock, and
J van Denderen, and
L A Aarden
April 1960,
Annals of the New York Academy of Sciences,
