Abstract
It is known that pituitary FSH, LH, and TSH are heterogeneous, existing as families of isoforms with respect to isoelectric point (pI), circulating half-life, in vitro and in vivo activities (for recent review, see [1]). To date, however, no systematic study has been undertaken to purify and characterize these isoforms with a view to establishing the biochemical basis for these differences. To this end, we have utilized a novel method exploiting the differences in charge-based protein separation between isoelectrofocusing and ion exchange chromatography for the purification to homogeneity of the isoforms of human pituitary FSH.
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References
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© 1992 Springer-Verlag New York, Inc.
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Stanton, P.G., Robertson, D.M., Burgon, P.G., White, B., Hearn, M.T.W. (1992). Purification and Biological Activities of Isoforms of Human FSH. In: Hunzicker-Dunn, M., Schwartz, N.B. (eds) Follicle Stimulating Hormone. Serono Symposia USA. Springer, New York, NY. https://doi.org/10.1007/978-1-4684-7103-8_32
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DOI: https://doi.org/10.1007/978-1-4684-7103-8_32
Publisher Name: Springer, New York, NY
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