• Fisheries and Aquatic Sciences
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• v.24 no.4
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• pp.163-170
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• 2021

Peptides are naturally occurring biological molecules that are found in all living organisms. These biologically active peptides play a key role in various biological processes. The aim of this study is the extraction and the purification of bioactive materials that induce relaxation of an apical muscle from the pyloric caeca of Patiria pectinifera. The acidified pyloric caeca extract was partially separated by the solid phase extraction using a stepwise gradient on Sep-Pak C18 cartridge. Among the fractions, materials eluted with 60% methanol/0.1% trifluoroacetic acid was put a thorough of a series of high performance liquid chromatography (HPLC) steps to isolate a neuropeptide with relaxation activity. The purified compound was eluted at 28% acetonitrile in 0.1% trifluoroacetic acid with retention time of 25.8 min on the CAPCELL-PAK C18 reversed-phase column. To determine the molecular weight and the amino acid sequence of the purified peptide, LC-MS and Edman degradation method were used, respectively. The primary structure of the peptide was determined to be FGMGGAYDPLSAGFTD which corresponded to the amino acid sequence of a starfish myorelaxant peptide (SMP) isotype (SMPb) found in the cDNA sequence encoding SMPa and its isotypes. In this study, a muscle relaxant neuropeptide (SMPb) has been isolated from pyloric caeca of starfish P. pectinifera. This is the first report of SMPb isolation on the protein level from P. pectinifera.

• Fisheries and Aquatic Sciences
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• v.25 no.11
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• pp.572-578
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• 2022

An organism's physiological processes and behaviors are regulated by neuropeptides and hormone peptides. The first neuropeptide identified from echinoderms is SALMFamide. The two most well-studied SALMFamide neuropeptides are S1 and S2, which possess myoactivity on apical muscle, tube feet, and the cardiac stomach of starfishes. However, neuropeptide candidates identified from SALMFamide's precursor protein sequence have not been investigated. This study aims to compare the bioactivity of SALMFamide neuropeptides from the starfish Asterias rubens using various starfish muscle preparations. In this study, the bioactivity of the L-type SALMFamide neuropeptides from the starfish A. rubens, AYHTGLPFamide (SALMFa-A) and the derivative AYHSALMFamide (SALMFa-B) was investigated. The neuropeptides were applied on Asterias amurensis apical muscle, tube feet, which revealed that the neuropeptides exhibit relaxing activity on apical muscle but no activity on tube feet. The native SALMFa-A peptide had lower relaxing activity on the apical muscle compared to the derivative peptide SALMFa-B. The relaxing activity of two neuropeptides also was compared with those on the apical muscle of Patiria pectinifera, which revealed relaxing activity as well as SALMFamide-S1 and S2 neuropeptides. Moreover, the investigation of SALMFa-A and SALMFa-B peptides' bioactivity on P. pectinifera cardiac stomach muscle also showed slight relaxing activity.