• Title/Summary/Keyword: Hagfish

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Purification of a Bradykinin-Related Peptide from the Skin of Hagfish. Eptatretus burgeri (먹장어 (Eptatretus burgeri)의 피부로부터 Bradykinin-Related Peptide의 정제)

  • SHIN Mi Jung;KIM Eun Jung;KIM Chan-Hee;GO Hye-Jin;KIM In Hae;RYU Hong-Soo;Huh Min-Do;CHUNG Joon-Ki;PARK Nam Gyu
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.36 no.1
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    • pp.30-34
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    • 2003
  • A hagfish bradykinin(BK)-related peptide was isolated and characterized from the skin of hagfish, Eptatretus burgeri. The hagfish BK with a molecular mass of 875.8 Da was purified to a homogeneity using $C_{18}$ reverse-phase and cation-exchange high performance liquid chromatography. The primary structure of the hagfish BK was determined as Gly-Thr-Ala-Gly-Ile-Gly-Pro-Phe-Arg by a combination of an automated amino acid sequencing and MALDI-TOF mass spectrometry. This amino acid sequence contains five substitutions $(Arg^1{\rightarrow}Gly,\;Pro^2{\rightarrow}Thr,\;Pro^3{\rightarrow}Ala,\;Phe^5{\rightarrow}Ile,\;Ser^6{\rightarrow}Gly)$ compared with that of mammalian BK. The hagfish BK showed a contractile action on the intestine of hagfish, Eptatretus burgeri. The threshold concentration of hagfish BK was around $10^{-11}\;M.$

Effects of Water Temperature and Salinity on Blood Properties and Oxygen Consumption in Hagfish (Eptatretus burgeri) (먹장어(Eptatretus burgeri)의 혈액성상과 산소소비에 미치는 수온 및 염분의 영향)

  • Do, Yong-Hyun;Min, Byung-Hwa;Myeong, Jeong-In;Jee, Young-Ju;Chang, Young-Jin
    • Journal of Fisheries and Marine Sciences Education
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    • v.26 no.1
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    • pp.214-222
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    • 2014
  • Hagfish Eptatretus burgeri is classified as a agnathans and has many different physiological properties compared with vertebrates. In this study, we examined effects of water temperature and salinity on blood properties and oxygen consumption in hagfish. In the experiment of water temperature change, hematocrit (Ht), red blood cell (RBC) and glucose of hagfish blood revealed the lowest values at $15^{\circ}C$. Oxygen consumption of hagfish had significantly increased with rising water temperature, and the increasing rate was twice as much when the temperature was manipulated every $5^{\circ}C$. Also, oxygen consumption during the night time (a short photoperiod) was significantly higher than that of the daytime. Q10 level was 3.50 in the light period and 3.92 in the dark period. No significant change in plasma glucose level was showned in changing salinity from 30 psu to 22 psu, while it had rapidly increased at 20 psu ($13.7{\pm}4.0mg/dL$) and thereafter all hagfish were dead at 18 psu. However, osmolarity, $Na^+$, $K^+$ and $Cl^-$ levels had significantly decreased when salinity decreased. This results are expected to develop the artificial rearing techniques of natural hagfish.

Protein Quality Evaluation of Cooked Hagfish (Eptatretus burgeri) Meats

  • Hwang, Eun-Young;Lee, Jin-Hwa;Ryu, Hong-Soo;Park, Nam-Gyu;Chun, Soon-Sil
    • Preventive Nutrition and Food Science
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    • v.7 no.3
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    • pp.287-292
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    • 2002
  • The effect of cooking methods on in vivo and in vivo indices of the protein quality of hagfish meat were investigated. In vivo protein digestibilities of cooked meats (81.3~83.5 %) were not significant different (p<0.05) from those of van meat (82.9%), with the exception of steamed (11$0^{\circ}C$, 15 min) meat (86.3 %). Convection oven cooking (22$0^{\circ}C$, IS min) resulted in a higher trypsin indigestible substrate (TIS, 49.2 mg/g solid) compared with that of raw meat (38.9 mg/g solid). free amino acid content of raw meat was decreased after boiling (10$0^{\circ}C$, 10min). Both convection oven and microwave cooking (2,450 MHz, 3 min) decreased available lysine from 4.9g/16g N to 3.8~4.1g/16g N. In vivo apparent protein digestibilites (AD) of hagfish meat were similar fur raw (92.4%) and cooked meats, but were somewhat lower than ANRC (Animal Nutrition Research Council) casein (945%). The PERs (3.7~4.1) and NPRs (3.7~4.9) of cooked meats were significantly higher (p<0.05) than those of raw meat (PER 3.3, NPR 3.6 and ANRC casein (PER 2.5, NPR 2.6), despite their lower in vivo protein digestibilities. These results demonstrate that cooking at optimal conditions resulted in remarkably positive effects on in vivo and in vivo protein qualities of hagfish meats. Therefore, steamed hagfish meat is an excellent source of high quality protein from seafood products.

Reproduction characteristics of hagfish Eptatretus burgeri in the South Sea of Korea (한국 남해에 출현하는 먹장어 Eptatretus burgeri의 재생산 특성)

  • KIM, Doo-Nam;HWANG, Kang-Seok;CHA, Hyung-Kee;PARK, Jun-Su;KIM, Jung-Nyun;MOON, Seong-Yong;LEE, Jeong-Hoon
    • Journal of the Korean Society of Fisheries and Ocean Technology
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    • v.54 no.2
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    • pp.188-192
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    • 2018
  • The reproduction characteristics of hagfish Eptatretus burgeri were examined using individuals caught in the South Sea of Korea. The spawning season and size at minimum sexual maturity of this species were characterized based on a gonad-somatic index (GSI) and monthly variation egg size (long axis). From monthly variation of GSI, the spawning season was estimated to be from August to September. Developing eggs larger than 10 mm were found in March, and the largest egg size was found in July. The first spawning length was 34.2 cm TL. Batch fecundity ranged from 13 to 117 eggs for hagfish sized from 34.2 cm TL to 77.0 cm TL, respectively, and increased linearly with total length.

Purification of Neuropeptide with the Contractile Activity on the Smooth Muscle from the Skin of Conger Eel Conger myriaster (붕장어(Conger myriaster)의 피부로부터 평활근 수축작용을 지닌 신경성 펩타이드의 정제)

  • Go, Hye-Jin;Park, Nam-Gyu
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.45 no.4
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    • pp.358-366
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    • 2012
  • A novel neuropeptide was isolated from the skin of the conger eel Conger myriaster using hagfish Eptatretus burgeri intestine as a bioassay system. The sequence of the purified peptide was analyzed using automated amino acid sequencing and MALDI-TOF mass spectrophotometry. The molecular ion peak in the MALDI-TOF mass spectrum of the peptide was at m/z 962.89 $(M+H)^+$. The sequence of the peptide was determined to be L-P-M-L-E-T-Q-M, and was tentatively named comyrin. To investigate the complete primary structure of comyrin, comyrin-OH and comyrin-$NH_2$ were synthesized and the chemical and pharmacological properties of the synthetic peptides were compared with those of the native peptide. However, the elution time of synthetic peptides did not match that of the native peptide on the reverse-phase HPLC chromatogram. In addition, the synthetic peptides did not cause contractile activity in the intestinal smooth muscle of the hagfish. Based on these results, one possible reason for this disagreement may be the presence of a D-amino acid in comyrin.

Purification and Characterization of Novel Antimicrobial Peptide from the Skin of the Hagfish , Eptatretus burgeri

  • Hwang, Eun-Young;Seo, Jung-Kil;Kim, Chan-Hee;Go, Hye-Jin;Kim, Eun-jung;Chung, Joon-Ki;Rye, Hong-Soo;Park, Nam-Gyu
    • Preventive Nutrition and Food Science
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    • v.4 no.1
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    • pp.28-32
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    • 1999
  • A novel antimicrbial peptide , named HFS-I, was isolated and characterized from the skin of the hagfish, Eptatretus bugeri. The decapeptide with a molecular mass of 1279.5 Da was purified to homogeneity using a gel-filtration column, ion-exchange and C18 reverse-phase high performance liquid chromatograpy . The complete amino acid sequence of HFS-I, which was determined by a combination of an automated amino acid sequencing and FAB-MS, was F-P-W-W-L-S-G-K-Y-P-NH2. Comparison of the amino acid sequence with those of other known antimicrobial peptides revealed that HFS-I was a novel antimicrobial peptide. HFS-I showed a weak antimicrobial activity in vitro aganinst a broad spectrum of microorganism without hemolytic acitivity.

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Cloning, Expression Analysis and Enzymatic Characterization of Cathepsin L from the Inshore Hagfish (Eptatretus burgeri) (먹장어 Cathepsin L의 분자생물학적 클로닝, 발현 및 효소학적 특성 분석)

  • JANG, Jin-Hyeon;SON, So-Hee;JO, Hyeon-Kyeong;CHUNG, Joon-Ki;LEE, Hyung-Ho
    • Journal of Fisheries and Marine Sciences Education
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    • v.28 no.4
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    • pp.903-912
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    • 2016
  • Hagfish which belongs to the chordate contact cyclostomata, is important phylogenetic relationship between vertebrate and invertebrate. Cathepsins of the cysteine protease family have traditionally been thought to play a major role in intracellular protein degradation and turnover in lysosomes. In this study, Catepsin L was cloned from Inshore hagfish (Eptatretus burgeri), the cDNA encoding ORF of the Eptatretus burgeri Cathepsin L (EbCtL) is 978 bp. The cDNA encoding proEbCtL was expressed in Escherichia coli strain BL21(DE3) using the pGEX-4T-1 expression vector system. The recombinant proEbCtL protein was overexpressed as a approximately 55 kDa fusion protein. The overproduced soluble GST-fusion protein was then applied to glutathione-Sepharose 4B column chromatography; the sample harboring the fusion protein evidenced a high degree of purity when analyzed via SDS-PAGE and Western blot analysis. Its activity was quantied by cleaving the synthetic peptide Z-FR-AMC, Z-LLE-AMC, and Suc-AAF-AMC, and the optimal pH for the protease activity was 8, 9.5, and 9, respectively.

Fatty Acid Combination of Major Triglyceride in Hagfish Flesh Lipids (먹장어 지질의 주된 트리글리세리드의 지방산조성)

  • LEE Eung-Ho;WADA Shun;KOIZUMI Chiaki;OHSHIMA Toshiaki;NONAKA Junsaku
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.17 no.4
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    • pp.291-298
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    • 1984
  • The extracted hagfish (Eptatretus burgeri) flesh lipid was separated into following fractions by column chromatography on Bio-beads SX-2 and Sephadex LH-20 prior to gab chromatographic analysis of their fatty acid compositions: polar lipid, triglyceride and free fatty acid. The major fatty acids of total lipid and triglyceride in hagfish were $C_{16:0},\;C_{16:1},\;and\;C_{18:1}$. The ratio of $C_{18:0}/C_{18:1}$ in the total lipid and triglyceride of hagfish was 0.1. The polar lipid of the hagfish muscle was mainly composed of phosphatidyl choline ($65.5\%$) and phosphatidyl ethanolamine ($28.0\%$). The triglyceride obtained was fractionated into four fractions by HPLC on the basis of partition numbers. Both the fatty acid composition and triglyceride composition on the basis of the total carbon number in the acyl chains of the triglyceride were analysed by the GLC. From the information obtained on triglyceride compositions based on the total carbon number by GLC and the partition number by HPLC and fatty acid composition by GLC, the combination of fatty acid in each triglycerides was estimated. A computer was used for estimation of the fatty acid combination in the triglyceride because hagfish lipid triglyceride was composed of various kinds of fatty acids. Fortyfour kinds of triglyceride were estimated. The major triglycerides in hagfish flesh lipid were found to those of ($1{\times}C_{16:0},\;2{\times}C_{18:1};\;13.5\%$), ($1{\times}C_{16:0},\;1{\times}C_{18:0},\;1{\times}C_{18:1};\;7.2\%$), ($1{\times}C_{16:1},\;2{\times}C_{18:1};\;5.4\%$), ($2{\times}C_{16:0},\;1{\times}C_{22:5};\;5.2\%$), ($1{\times}C_{14:0},\;2{\times}C_{18:1};\;4.5\%$), ($2{\times}C_{18:1},\;1{\times}C_{22:5};\;3.6\%$), ($1{\times}C_{14:0},\;1{\times}C_{18:0},\;1{\times}C_{18:1};\;2.7\%$) and ($1{\times}C_{14:0},\;1{\times}C_{16:0},\;1{\times}C_{18:2};\;2.2\%$).

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CONDITIONS FOR CONGER EEL AND HAGFISH SKIN GLUE PROCESSING AND THE QUALITY OF PRODUCT (붕장어피 및 먹장어피를 이용한 피교의 가공조건에 제품의 성상)

  • LEE Eung-Ho;KIM Se-Kwon;CHO Duck-Jae;KIM Jin-Dong;no Sudibjo;KIM Soo-Hyun
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.11 no.4
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    • pp.189-195
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    • 1978
  • Using the skins of conger eel, Astroconger myriaster, and hagfish, Eptatretus burzeri, from fillet manufactory, the optimum conditions of skin glue processing were investigated and physical ana chemical properties of the product were also determined. The yields of conger eel and hagfish skin to the total body weight were $10.6\%$ and $11.4\%$, respectively. The optimum processing conditions for conger eel skin glue were the extraction of skins which were previously tinted with $0.3\%$ calcium hydroxide solution for one hour, in water at pH 5.5 and $60^{\circ}C$ for four hours. The additional water was six times sample weight. In case of the hagfish skin glue, the liming time with $0.3\%$ calcium hydroxide solution was suitable for three hours, and the skins were extracted with water as much as nine times sample weight at pH 5.0 and $60^{\circ}C$ for three hours. The contents of crude protein of conger eel and hagfish skin glue were $91.5\%$ and $90.2\%$, respectively. The content of crude lipid was slightly higher than that of chemical grade gelatin. Relative viscosity, melting point, gelation temperature and jelly strength of conger eel skin glue were 13.6, $15.2^{\circ}C$, $6.2^{\circ}C$ and 13.0g respectively and those of hagfish skin glue were 12.9, $14.8^{\circ}C$, $4.3^{\circ}C$ and 23.3g respectively. The turbidity of conger eel skin glue and hagfish skin glue were slightly superior to those of dry glue.

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PROCESSING OF STEAMED FISH JELLY PRODUCT FROM HAGFISH (먹장어 어묵 제조)

  • KIM Soo-Hyun
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.11 no.4
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    • pp.197-203
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    • 1978
  • In this study, the effects of some additives to the quality of fish jelly product such as salt tripolyphosphate and starch were examined. Besides, that of washing and stepwise heating procedure were also discussed. From the result of quality test by measuring jelly strength and sensory evaluation the product was quite palatable 19 common, and the addition of 3 percent of salt and 5 percent of starch resulted in the best jelly strength. It was markedly enforced when 0.3 percent of tripolyphosphate was added. The suggestible processing method of hagfish jelly product is as follows : The meat is to be bleached by washing at least 6 times with tenfold tap water by volume of meat at $5-6^{\circ}C$ and then ground throughly with addition of 3 percent of salt, 5 percent of starch and 0.3 percent of tripolyphosphate. The ground meat is finally to be heated for 1 hour at 45 to $50^{\circ}C$ and then for 30 minutes at $90^{\circ}C$.

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