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김찬희,고혜진,Eun Jung Kim,서정길,홍용기,김형락,정준기,Yojiro Muneoka,박남규 대한화학회 2006 Bulletin of the Korean Chemical Society Vol.27 No.11
A new biologically active peptide with structural similarity to neuromedin N (NMN) has been isolated from extracts of visceral tissue of the African lungfish, Protopterus dolloi, using the rectum of the quail as the bioassay system. The primary structure of NMN-related peptide was established as Lys-Ala-Pro-Tyr-Ile-Leu-OH ([Ala2]-NMN) and contained one substitution (Ala2 Ile) compared with the porcine NMN. [Ala2]-NMN was found to have an excitatory effect on rectal muscle tissues of quail (Coturnix japonica), newt (Cynops pyrrhogaster) and black bass (Micropterus sulmoides). The threshold concentration of [Ala2]-NMN for contraction of C. japonica muscle was found to be approximately 10-11 M. [Ala2]-NMN showed contractile activities in the following order: C. japonica > C. pyrrhogaster > M. sulmoides. The identification of [Ala2]-NMN provides evidence that NMN family, hitherto confined to mammals, has a widespread occurrence in lungfish.
김찬희,Eun Jung Kim,고혜진,Hyung Ho Lee,홍용기,Hyung-Rak Kim,Joon Ki Chung,박장수,Yojiro Muneoka,박남규 대한화학회 2006 Bulletin of the Korean Chemical Society Vol.27 No.7
The peptide with structural similarity to mammalian substance P (M-SP) has been isolated from extract of the body of the African lungfish, Protopterus dolloi, using the rectum of the newt as the bioassay system. The primary structure of the SP-related peptide was identified as Lys-Pro-Arg-Pro-Asp-Gln-Phe-Tyr-Gly-Leu-Met-NH2 (L-SP) and contained four substitutions (Lys1 Arg, Arg3 Lys, Asp5 Gln, and Tyr8 Phe) compared with M-SP; this structure is identical to that of the peptide isolated from the gut of the Australian lungfish. Circular dichroism spectra showed that L-SP had an unordered structure in the buffer solution and phospholipid bilayers. This peptide was found to have an excitatory effect on rectal muscle tissues of newt, quail, and fish. L-SP also had a more potent vasodilatory effect on the guinea-pig aorta than that of M-SP. The identification of the peptide provides evidence that SP family, hitherto confined to mammals, have a widespread occurrence in lungfish.
Kim, Chan-Hee,Kim, Eun-Jung,Go, Hye-Jin,Lee, Hyung-Ho,Hong, Yong-Ki,Kim, Hyung-Rak,Chung, Joon-Ki,Park, Jang-Su,Muneoka, Yojiro,Park, Nam-Gyu Korean Chemical Society 2006 Bulletin of the Korean Chemical Society Vol.27 No.7
The peptide with structural similarity to mammalian substance P (M-SP) has been isolated from extract of the body of the African lungfish, Protopterus dolloi, using the rectum of the newt as the bioassay system. The primary structure of the SP-related peptide was identified as Lys-Pro-Arg-Pro-Asp-Gln-Phe-Tyr-Gly-Leu-Met-NH2 (L-SP) and contained four substitutions ($Lys^{1}\rightarrow $ Arg, $Arg^{3}\rightarrow$ Lys, $Asp^{5}\rightarrow$ Gln, and $Tyr^{8}\rightarrow$ Phe) compared with M-SP; this structure is identical to that of the peptide isolated from the gut of the Australian lungfish. Circular dichroism spectra showed that L-SP had an unordered structure in the buffer solution and phospholipid bilayers. This peptide was found to have an excitatory effect on rectal muscle tissues of newt, quail, and fish. L-SP also had a more potent vasodilatory effect on the guinea-pig aorta than that of M-SP. The identification of the peptide provides evidence that SP family, hitherto confined to mammals, have a widespread occurrence in lungfish.
Kim, Chan-Hee,Go, Hye-Jin,Kim, Eun-Jung,Seo, Jung-Kil,Hong, Yong-Ki,Kim, Hyung-Rak,Chung, Joon-Ki,Muneoka, Yojiro,Park, Nam-Gyu Korean Chemical Society 2006 Bulletin of the Korean Chemical Society Vol.27 No.11
A new biologically active peptide with structural similarity to neuromedin N (NMN) has been isolated from extracts of visceral tissue of the African lungfish, Protopterus dolloi, using the rectum of the quail as the bioassay system. The primary structure of NMN-related peptide was established as Lys-Ala-Pro-Tyr-Ile-Leu-OH ([$Ala_2$]-NMN) and contained one substitution ($Ala_2\rightarrow$Ile) compared with the porcine NMN. [$Ala_2$]-NMN was found to have an excitatory effect on rectal muscle tissues of quail (Coturnix japonica), newt (Cynops pyrrhogaster) and black bass (Micropterus sulmoides). The threshold concentration of [Ala2]-NMN for contraction of C. japonica muscle was found to be approximately $10^-11$M. [$Ala_2$]-NMN showed contractile activities in the following order: C. japonica > C. pyrrhogaster > M. sulmoides. The identification of [Ala2]-NMN provides evidence that NMN family, hitherto confined to mammals, has a widespread occurrence in lungfish.