Abstract：
:Human seminal fluid contains a number of tripeptide amides with similar structures to thyrotropin releasing hormone (TRH), two of which have been identified as pGlu-Glu-Pro amide and pGlu-Phe-Pro amide. To determine whether these peptides originate in the same tissues and have the same molecular origin, TRH-immunoreactive peptides were extracted from the prostate and testis of the rabbit, purified by ion exchange chromatography and HPLC, and identified by co-chromatography with 3H-labelled marker peptides. In addition, trypsin digestion was used to release TRH-like tripeptides from N-extended forms of these peptides. The sole TRH-like peptide in the prostate was shown to be pGlu-Glu-Pro amide; it was not accompanied by a detectable amount of pGlu-Phe-Pro amide. The prostate also appeared to contain a very small amount of N-extended forms of these peptides. In contrast to the prostate, the testis contained high concentrations of N-extended forms of pGlu-Phe-Pro amide but essentially no tripeptide. The testis also contained N-extended forms of two other neutral TRH-like peptides which were less hydrophobic than pGlu-Phe-Pro amide. Neither the prostate nor the testis contained a significant amount of TRH. The results show that in the rabbit the TRH-like peptides pGlu-Glu-Pro amide and pGlu-Phe-Pro amide occur in different tissues and appear to be formed from different precursors.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Linden H,del Rio Garcia J,Huber A,Kreil G,Smyth Ddoi
10.1016/0014-5793(95)01468-3subject
Has Abstractpub_date
1996-01-22 00:00:00pages
11-4issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(95)01468-3journal_volume
379pub_type
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