TRH-related peptides in the rabbit prostate complex during development
| Autor: | Caroline R. Thetford, Sheena M. Cockle, Jane M. Morrell |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Male
endocrine system medicine.medical_specialty Aging Ion chromatography Size-exclusion chromatography Molecular Sequence Data Biophysics Peptide Tripeptide Peptide hormone Biochemistry Bulbourethral gland Prostate Internal medicine medicine Animals Trypsin Amino Acid Sequence Sexual Maturation Molecular Biology Thyrotropin-Releasing Hormone chemistry.chemical_classification Chemistry Radioimmunoassay Chromatography Ion Exchange Peptide Fragments Pyrrolidonecarboxylic Acid medicine.anatomical_structure Endocrinology Chromatography Gel Rabbits Oligopeptides hormones hormone substitutes and hormone antagonists |
| Zdroj: | Biochimica et biophysica acta. 1115(3) |
| ISSN: | 0006-3002 |
| Popis: | The novel peptide, pyroglutamylglutamylprolineamide (pGlu-Glu-ProNH2), has recently been isolated and characterized from the rabbit prostate complex. The tripeptide is present in high concentrations in the prostate complex and semen, together with a 40–50 residue polypeptide which contains a TRH-immunoreactive fragment at its C-terminus. The present study investigates changes in the levels of these TRH-related peptides in rabbits aged 11 weeks, 4 months, 7 months, 13 months and 2 years. For each age group the peptides were extracted from the prostate complex, separated by gel exclusion chromatography, and located by TRH radioimmunoassay. The TRH-immunoreactive fragment was released from the polypeptide by trypsin digestion prior to radioimmunoassay. Very low concentrations of TRH-immunoreactive peptides were present at 11 weeks of age, but considerable levels of both peptides were found in all the other age groups. Anion exchange chromatography, under conditions which resolve TRH and pGlu-Glu-ProNH2, showed that the majority of the low molecular weight TRH immunoreactivity co-eluted with synthetic pGlu-Glu-ProNH2. The remaining TRH immunoreactivity, which had not bound to the anion resin, also failed to bind to a cation exchange column at pH 2.0, indicating that it was not authentic TRH. Dissection of the prostate complex into its four constitutive regions (vesicular gland, coagulating gland, prostate and bulbourethral gland) followed by extraction, chromatography and TRH radioimmunoassay of each region showed that the TRH-related peptides were located in the prostate. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|