FEBS Letters | |
Characterization of a cDNA encoding a precursor of Carassius RFamide, structurally related to a mammalian prolactin‐releasing peptide | |
Minakata, Hiroyuki1  Satake, Honoo1  Fujimoto, Masaaki2  Wang, Xiaoyan2  | |
[1] Suntory Institute for Bioorganic Research, Wakayamadai 1-1-1, Shimamoto-cho, Mishimagun, Osaka 618-8503, Japan;Department of Biological Science, Faculty of Life and Environmental Science, Shimane University, Nishikawatsu-cho 1060, Matsue 690-8504, Japan | |
关键词: RFamide; Precursor; Expression; Carassius auratus langsdorfi; ACEP-1; Achatina cardioexcitatory peptide; C-RFa; Carassius RFamide; DIG; digoxigenin; HCIP; Helix cardioinhibitory peptide; LyCEP; Lymnaea cardioexcitatory peptide; PrRP; prolactin-releasing peptide; RACE; rapid amplification of cDNA end; RT-PCR; reverse transcription-polymerase chain reaction; | |
DOI : 10.1016/S0014-5793(99)00215-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
We have characterized the cDNA encoding Carassius RFamide (C-RFa), which is structurally related to mammalian prolactin-releasing peptides (PrRPs), from the brain of the crucian carp. The deduced C-RFa precursor has been shown to comprise 117 amino acids, encoding a single C-RFa sequence. A comparative study of amino acid sequences has revealed that several sequences conserved in preproPrRPs are also found in the C-RFa precursor. Furthermore, the abundant presence of the C-RFa mRNA in the telencephalon, optic tectum, medulla oblongata, and proximal half eye ball was demonstrated by Southern blot analysis of RT-PCR products.
【 授权许可】
Unknown
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