Abstract
Acetic acid extracts of codfish brain contain three different immunoreactive (IR) luteinizing hormone-releasing hormone (LH-RH) like materials which differ from the mammalian LH-RH decapeptide by their behavior on chromatographic separation (molecular sieving, ion exchange and high performance liquid chromatography), and their reaction with two well characterized antisera directed against different regions of the LH-RH molecule. One of the IR LH-RH like substances is a larger molecular weight compound (1800 to 4,000 daltons), which may be a precursor of LH-RH extended at the N-terminus. The other two are approximately the same size as mammalian LH-RH and their nature is best explained by the occurrence of single amino acid substitutions at the C-terminal region of the ‘authentic’ decapeptide.
Published Version
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