The α and β subunits of ovine and bovine gonadotrophins which undergo instant dissociation in 0·1% (v/v) trifluoroacetic acid in water could be separated into their multiple components by reverse-phase high-performance liquid chromatography on analytical and preparative scales. Several batches of highly purified ovine LH (oLH) separated into four α components (α1 to α4) and five β components (β1 to β5). While the major α component (α3) remained the same in all, the β subunit was variable in all these prepartions of oLH of equal biological and immunoreactivity. Various manipulations, such as prolonged incubation in dilute acid or alkali or conditions prone to air oxidation, did not change elution patterns or produce interconversions among the α or β components, suggesting that microheterogeneity arose in the pituitary itself or during its collection. The subunits obtained on a preparative scale were of high yield and quality and recombined (100%) to produce fully active LH or FSH. Chemical deglycosylations in which 75–80% of the peripheral sugars were removed shifted the elution of all components (a as well as β) slightly but modifications to the protein backbone by other reagents changed the profile of the α subunit. Obtaining the various α and β components in high yield would permit a complete analysis of gonadotrophin microheterogeneity.
Journal of Endocrinology (1991) 130, 415–424
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