Molecular cloning of follicle-stimulating hormone (FSH)-β subunit cDNA from duck pituitary
| Autor: | Tzu-Yun Shen, John Yuh-Lin Yu, Yi-Sheng Cheng, San-Tai Shen |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Male
Models Molecular Signal peptide Pituitary gland DNA Complementary Molecular Sequence Data Molecular cloning Biology Follicle-stimulating hormone Endocrinology Complementary DNA medicine Animals Nucleotide Amino Acid Sequence Cloning Molecular Peptide sequence Phylogeny chemistry.chemical_classification Base Sequence Sequence Homology Amino Acid Reverse Transcriptase Polymerase Chain Reaction Molecular biology Protein Subunits Ducks medicine.anatomical_structure chemistry Glycoprotein Hormones alpha Subunit Pituitary Gland Follicle Stimulating Hormone beta Subunit Animal Science and Zoology Follicle-stimulating hormone receptor |
| Zdroj: | General and Comparative Endocrinology. 148:388-394 |
| ISSN: | 0016-6480 |
| DOI: | 10.1016/j.ygcen.2006.03.013 |
| Popis: | We have cloned FSH-beta cDNA from duck pituitary gland by reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA end (RACE) methods. The cloned duck FSH-beta cDNA contains 1909-bp nucleotides including 396-bp of open-reading frame and 1491-bp of 3'-untranslational region. The open-reading frame encodes a 131-amino acid protein with a putative 20-amino acid signal peptide and a putative 111-amino acid mature protein. The deduced amino acid sequence shows a remarkable similarity (94-98%) to those of other avian FSH-beta subunits; while it exhibits lower similarities with those of turtles (82-84%), mammals (63-71%), and amphibians (53-57%). The structural model analysis of duck FSH suggests that the cysteine-knot and beta-strands for maintaining the specific structural frame, and the "seat-belt" loop for specific binding to FSH receptor have been conserved in tetrapodian FSH-betas. |
| Databáze: | OpenAIRE |
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