Abstract:
:In light of current discussions on multiple forms of inhibin, it was thought of interest to ascertain the identity of the postulated 'iso-hormones' of bull seminal plasma inhibin (Chari et al., 1978). By subjecting the biologically active fraction, obtained by Sephadex G-100 gel filtration of bull seminal plasma acetone powder, to extensive dialysis in distilled water adjusted to pH 5.8, it was possible to remove the bulk of inert protein as a precipitate. The resulting active preparation could be readily fractionated by preparative iso-electric focusing in the pH range 4.0-6.5 yielding 2 distinct homogeneous peptides, alpha and beta, capable of suppressing hCG-induced uterine weight increase in immature mice, in a 'reversed Steelman-Pohley' assay design. However, of these, alpha alone was able to suppress post-castrational serum gonadotropin rise in appropriate animal models. This peptide is highly acidic in nature (iso-electric point congruent to 2.2) and has a molecular weight (Mr) of 18200 and a Stokes radius of 1.90 nm. On the basis of currently available evidence, it is concluded that the molecule consists of a single peptide chain.
journal_name
Mol Cell Endocrinoljournal_title
Molecular and cellular endocrinologyauthors
Mohapatra SK,Duraiswami S,Chari Sdoi
10.1016/0303-7207(85)90022-xsubject
Has Abstractpub_date
1985-07-01 00:00:00pages
187-96issue
2-3eissn
0303-7207issn
1872-8057journal_volume
41pub_type
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