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Biology of Reproduction, Vol 51, 63-71, Copyright © 1994 by Society for the Study of Reproduction

ARTICLES

Initial characterization of equine inhibin

KH Moore, BS Dunbar, GR Bousfield and DN Ward
Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

Inhibin has been characterized from a number of mammals; however, it has not been extensively studied in horses. Western blot analysis was used to examine the size heterogeneity of equine inhibin alpha- and beta-subunits. The distribution of equine inhibin activity from the initial sizing column (S-200, 25 x 94 cm) indicated that the majority of equine inhibin activity was present as larger-molecular-size forms. When the large forms were analyzed by Western blot in nonreducing conditions, alpha-subunit bands were detected at 40,000 M(r), 56,000 M(r), 80,000 M(r), and 90,000 M(r); beta a reactive bands were identified at 56,000 M(r) (strong) and 90,000 M(r) (faint). Western blot analysis of the lower-molecular-weight inhibins on one-dimensional (1D) SDS-PAGE gels revealed one inhibin band at 32,000 M(r). In reduced 1D-PAGE gels, a doublet alpha-subunit band was found at 18,000 M(r), and one beta a band was found at 14,000 M(r). The 18,000 M(r) equine alpha-subunit was present in three distinct spots in the isoelectric focusing (IEF) dimension of two-dimensional (2D)-PAGE, and closely overlapped those of porcine inhibin alpha-subunit. In conclusion, inhibin is present in good yield in equine follicular fluid. A higher proportion of the total activity is present in higher-molecular-weight forms than with porcine inhibin. Inhibin was detected at 90,000 M(r), 56,000 M(r), and 32,000 M(r). Alpha-subunit-only bands at 40,000 M(r) and 80,000 M(r) were detected. The lower-molecular-weight form of equine inhibin is similar to porcine inhibin in size and pattern on 2D- PAGE.


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