Initial characterization of equine inhibin
Date
1994-07-01Author
Moore, Katherine H.
Dunbar, Bonnie S.
Bousfield, George R.
Ward, Darrell N.
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K H Moore, B S Dunbar, G R Bousfield, D N Ward; Initial Characterization of Equine Inhibin; Biology of Reproduction July 1, 1994 vol. 51 no. 1 63-71; doi: 10.1095/biolreprod51.1.63
Abstract
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 a- and [S-subunits. The distribution of equine inhibin
activity from the initial sizing column (S-200, 25 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, -subunit bands
were detected at 40 000 M,, 56 000 Mr, 80 000 Mr, and 90 000 M,; Pa reactive bands were identified at 56 000 Mr (strong) and
90 000 M, (faint). Western blot analysis of the lower-molecular-weight inhibins on one-dimensional (ID) SDS-PAGE gels revealed
one inhibin band at 32 000 Mr. In reduced ID-PAGE gels, a doublet a-subunit band was found at 18000 M,, and one pa band
was found at 14 000 M,. The 18 000 M, equine a-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 a-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,, 56 000 M,, and 32 000 Mr. Alpha-subunit-only bands at
40 000 Mr and 80 000 M, 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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