IntroductionLuteinizing hormone fl subunits from ovine (0-LH 0) and bovine (B-LH /3) origins were shown to be completely homologous [ 1,2] .We recently reported [3] that porcine luteinizing hormone /3 subunit (P-LH /3) exhibits 15 amino acid replacements when compared to B-LH /I and 0-LH 3.In order to see whether such a difference does also exist between amino acid sequences of porcine and ovine LH (Y subunits [4,5], we present here the primary structure of P-LH (Y and compare it to 0-LH c!. peptides, eluted in the first peak, were further purified by chromatography on QAE-Sephadex A-25 (Pharmacia).as previously described [2].Peptides from the other peaks were separated by preparative high voltage electrophoresis and paper chromatography
No takes yet. Share an insight, caveat, or question.
Maghuin‐Rogister et al. (1972) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: