Relaxin-like peptide in ascidians. I. Identification of the peptide and its mRNA in ovary of Herdmania momus.
The ovaries of the ascidian Herdmania momus were extracted for relaxin. Relaxin immunoactivity was eluted from Sephadex G-50 in the position of authentic porcine ovarian relaxin and these fractions were parallel to porcine relaxin in an homologous porcine relaxin radioimmunoassay. Poly(A)+ RNA from ascidian ovaries hybridized to a 32P-labeled porcine relaxin B-chain 48 mer oligonucleotide probe. There was no hybridization with 32P-labeled probes of equal length but was rather directed to the B-chain of human relaxin or to two different regions of the C-peptide of porcine relaxin. We conclude that the ascidian ovary produces a relaxin-like molecule, possibly with greater homology in the B-chain to mammalian relaxins than in the C-peptide region.
Georges
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Laboratoire de Biologie Cellulaire Animale, Université J. Fourier, Grenoble I, France.
Tashima
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Yamamoto
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Bryant-Greenwood
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GD
D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D002852:Chromatography, Ion Exchange; D005260:Female; D008969:Molecular Sequence Data; D010053:Ovary / Q000378:metabolism*; D015347:RNA Probes; D012333:RNA, Messenger / Q000032:analysis* / Q000302:isolation & purification; D011863:Radioimmunoassay; D012065:Relaxin / Q000096:biosynthesis* / Q000302:isolation & purification; D014561:Urochordata / Q000378:metabolism*
D015347:RNA Probes; D012333:RNA, Messenger; D012065:Relaxin