Publications by authors named "L Leversha"

Inhibin-related proteins were identified in human follicular fluid following fractionation by gel permeation chromatography under neutral and acidic conditions, reversed-phase high performance liquid chromatography (HPLC) and preparative polyacrylamide gel electrophoresis. A number of molecular mass forms of inhibin (30-36 and 59-66 kDa) based on their in vitro biological and immunological activities were identified, of which 59-66 kDa inhibin was the predominant form. Bioactive fractions devoid of inhibin immunoactivity were also identified with molecular masses of 46 and 55 kDa.

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Two forms of inhibin with molecular weights of 65,000 and 30,000 (65 and 30 kD) were isolated from ovine follicular fluid using a combination of gel permeation chromatography, reversed-phase high-performance liquid chromatography and preparative polyacrylamide gel electrophoresis. The 65 kD form was partially purified approximately 315-fold whilst the 30 kD form was isolated as two isoforms (29 and 30 kD) of similar biological activity and in greater than 95% purity (1210-fold purification and 4.2% recoveries).

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A rapid 2-day quantitative assay for inhibin bioactivity based on FSH secretion from pituitary cells of immature female rats is described. The bioassay exhibited steeper slopes, improved precision and greater (fourfold) sensitivity compared with a previously established pituitary FSH cell content assay. Whole pituitary glands were used for the preparation of pituitary cells and the method for cell dispersion required a single enzymatic treatment with trypsin.

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Bovine follicular fluid was used as a source for the isolation of gonadal inhibin, the activity of which was monitored by the dose dependent suppression of the FSH content of cultured pituitary cells. The procedures presented result in over 3000-fold purification of the starting material and the purified inhibin has an apparent molecular weight of 56000. The purified inhibin can be dissociated under reducing conditions into two subunits with molecular weights of 44000 and 14000 daltons.

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Inhibin activity was measured by bioassay in follicular fluid of 99 individual ovine follicles ranging from 1 . 4 to 6 . 8 mm diameter (used to calculate volume) and in various stages of atresia.

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