HOME HELP CONTACT US SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Burgon, P. G. Articles by Hearn, M. T. W. Search for Related Content PubMed Articles by Burgon, P. G. Articles by Hearn, M. T. W.

In a recent study, a five- to eightfold range in human FSH radioreceptor activity (RRA) was documented for highly purified isoforms of FSH when the data were expressed on an FSH protein content basis as determined by amino acid analysis. This study examined the FSH in vitro bioactivity and immunoactivity of these preparations. FSH in vitro biological activity showed a five- to eightfold range in activity with a high correlation with the RRA values (r=0·82). A similar five- to eightfold range of values was obtained with a specific FSH radioimmunoassay and an FSH two-site immunoassay with high correlations again observed between each other, between each immunoassay and with either the in vitro bioassay or the RRA method (r=0·77–0·995). Although there was overall a close correlation between these assays, significant differences in ratios of activities between the in vitro bioassay and other methods were observed with highly purified FSH isoform preparations from different pI regions.

The high correlation between in vitro bioassay/RRA methods and immunoassay methods over a wide range of isoform specific activities suggests that these methods are detecting similar structural features on each isoform. It is thus concluded that these immunoassays are not solely measuring hormone mass based entirely on amino acid composition. This conclusion raises questions about ratio measurements of FSH, where immunoassay methods are presumed to measure total protein content, and their application in physiological situations and clinical practice.

Journal of Endocrinology (1993) 139, 511–518

This article has been cited by other articles:

				M. P. Rose, R. E. Gaines Das, and A. H. Balen Definition and Measurement of Follicle Stimulating Hormone Endocr. Rev., February 1, 2000; 21(1): 5 - 22. [Abstract] [Full Text]

				M. D'Antonio, F. Borrelli, A. Datola, R. Bucci, M. Mascia, P. Polletta, D. Piscitelli, and R. Papoian Biological characterization of recombinant human follicle stimulating hormone isoforms Hum. Reprod., May 1, 1999; 14(5): 1160 - 1167. [Abstract] [Full Text] [PDF]

				B. J. Arey, P. E. Stevis, D. C. Deecher, E. S. Shen, D. E. Frail, A. Negro-Vilar, and F. J. López Induction of Promiscuous G Protein Coupling of the Follicle-Stimulating Hormone (FSH) Receptor: A Novel Mechanism for Transducing Pleiotropic Actions of FSH Isoforms Mol. Endocrinol., May 1, 1997; 11(5): 517 - 526. [Abstract] [Full Text]