[보고서]해양생태계의 해적생물인 불가사리로부터 유용성 물질 회수 및 해양생태계 복원

박남규

보고서 정보

주관연구기관

부경대학교 산학협력단

연구책임자

박남규

참여연구자

이형호 , 고혜진 , 안상중 , 김나영 , 조은희 , 문지영 , 권민희 , 김혜림 , 우경은 , 성지혜 , 이아람 , 이정수 , 이용훈 , 이민정

보고서유형

최종보고서

발행국가

대한민국

언어

한국어

발행년월

2011-02

과제시작연도

2010

주관부처

환경부

사업 관리 기관

한국환경산업기술원

등록번호

TRKO201200001746

과제고유번호

1485008468

DB 구축일자

2013-05-20

표 Fig. 1. The contractile activity of various tissues' extracts on the starfish (Asterina pectinifera) DRM.
표 Fig. 2. The relaxant activity of various tissues' extracts on the starfish(Asterina pectinifera) DRM.
표 Fig. 3. Antimicrobial activity of various tissues' extracts against E . coli D31.
표 Antimicrobial activity of two starfish extracts against E. coli D31.
표 Fig. 4. Typical tracing illustrating the relaxing response of starfish (Asterina pectinifera) extracts. Each down arrow represents the sample applied to the starfish DRM. The precontraction was induced ACh, 5×10-7 M.
$Fig. 5. CM52 cation exchange chromatography of starfish extracts RM60. The RM60 was loaded onto CM52 (2.5 × 300 mm) column and eluted with a gradient of ammonium acetate (dotted line) at flow rate of 2.75 mL/min (pH 5.0). The black bar represents relaxing active fractions on the starfish DRM. The down arrow represents the sample applied to the starfish DRM.$ 표 Fig. 5. CM52 cation exchange chromatography of starfish extracts RM60. The RM60 was loaded onto CM52 (2.5 × 300 mm) column and eluted with a gradient of ammonium acetate (dotted line) at flow rate of 2.75 mL/min (pH 5.0). The black bar represents relaxing active fractions on the starfish DRM. The down arrow represents the sample applied to the starfish DRM.
$Fig. 6. Reverse-Phase HPLC profile of the active fraction A in Fig. 5. The fraction A in Fig. 5 was pooled and loaded onto Vydac C18 (9.2 × 250 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 3.0 mL/min. The black bar represents relaxing active fraction on the starfish DRM.$ 표 Fig. 6. Reverse-Phase HPLC profile of the active fraction A in Fig. 5. The fraction A in Fig. 5 was pooled and loaded onto Vydac C18 (9.2 × 250 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 3.0 mL/min. The black bar represents relaxing active fraction on the starfish DRM.
$Fig. 7. Anion-exchange HPLC chromatography of the active fraction in Fig. 6. The active fraction in Fig. 6 was pooled and loaded onto DEAE-5PW (7.5 × 75 mm) column and eluted with a linear gradient of 1.0 M NaCl (dotted line) in 10 mM Tris-HCl buffer (pH 8.8) at flow rate of 0.5 mL/min. The black bar represents relaxing active fractions on the starfish DRM.$ 표 Fig. 7. Anion-exchange HPLC chromatography of the active fraction in Fig. 6. The active fraction in Fig. 6 was pooled and loaded onto DEAE-5PW (7.5 × 75 mm) column and eluted with a linear gradient of 1.0 M NaCl (dotted line) in 10 mM Tris-HCl buffer (pH 8.8) at flow rate of 0.5 mL/min. The black bar represents relaxing active fractions on the starfish DRM.
$Fig. 8. Reverse-phase HPLC profile of the active fraction in Fig. 7. The active fraction in Fig. 7 was pooled and loaded onto Hypersil BDS C18 (2 × 125 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 0.5 mL/min. The black bar represents relaxing active fraction on the starfish DRM.$ 표 Fig. 8. Reverse-phase HPLC profile of the active fraction in Fig. 7. The active fraction in Fig. 7 was pooled and loaded onto Hypersil BDS C18 (2 × 125 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 0.5 mL/min. The black bar represents relaxing active fraction on the starfish DRM.
$Fig. 9. Cation exchange HPLC profile of the active fraction in Fig. 8. The active fraction in Fig. 8 was loaded onto SP-5PW (7.5 × 75 mm) column and eluted with a linear gradient of 1.0 M NaCl (dotted line) in 10 mM phosphate buffer solution (pH 6.0) at flow rate of 0.5 mL/min. The black bar represents relaxing active fraction on the starfish DRM.$ 표 Fig. 9. Cation exchange HPLC profile of the active fraction in Fig. 8. The active fraction in Fig. 8 was loaded onto SP-5PW (7.5 × 75 mm) column and eluted with a linear gradient of 1.0 M NaCl (dotted line) in 10 mM phosphate buffer solution (pH 6.0) at flow rate of 0.5 mL/min. The black bar represents relaxing active fraction on the starfish DRM.
$Fig. 10. Final purification of the active fraction in Fig. 9. The active fraction in Fig. 9 was loaded onto a Hypersil BDS C18 (2 × 125 mm) and eluted with isocratically 25% CH3CN in 0.1 % TFA at flow rate of 0.5 mL/min (A). The down arrow represents the sample applied to the starfish DRM (B). The molecular weight of single peak (down arrow) of Fig. 10A was determined by MALDI-TOF Mass spectra (C).$ 표 Fig. 10. Final purification of the active fraction in Fig. 9. The active fraction in Fig. 9 was loaded onto a Hypersil BDS C18 (2 × 125 mm) and eluted with isocratically 25% CH3CN in 0.1 % TFA at flow rate of 0.5 mL/min (A). The down arrow represents the sample applied to the starfish DRM (B). The molecular weight of single peak (down arrow) of Fig. 10A was determined by MALDI-TOF Mass spectra (C).
$Fig. 11. Reverse-phase HPLC profile of the active fraction B in Fig. 5. The active fraction B in Fig. 5 was loaded onto Vydac C18 (9.2 × 250 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 3.0 mL/min. The black bar represents relaxing active fractions on the starfish DRM. The down arrow represents the sample applied to the starfish DRM.$ 표 Fig. 11. Reverse-phase HPLC profile of the active fraction B in Fig. 5. The active fraction B in Fig. 5 was loaded onto Vydac C18 (9.2 × 250 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 3.0 mL/min. The black bar represents relaxing active fractions on the starfish DRM. The down arrow represents the sample applied to the starfish DRM.
$Fig. 12. Anion-exchange HPLC profile of the active fraction B-Ⅱ in Fig. 11. The active fraction B-Ⅱ in Fig. 11 was pooled and loaded onto DEAE-5PW (7.5 × 75 mm) column and eluted with a linear gradient of 1.0 M NaCl (dotted line) in 10 mM Tris-HCl buffer (pH 9.2) at flow rate of 0.5 mL/min. The black bar represents relaxing active fractions on the starfish DRM.$ 표 Fig. 12. Anion-exchange HPLC profile of the active fraction B-Ⅱ in Fig. 11. The active fraction B-Ⅱ in Fig. 11 was pooled and loaded onto DEAE-5PW (7.5 × 75 mm) column and eluted with a linear gradient of 1.0 M NaCl (dotted line) in 10 mM Tris-HCl buffer (pH 9.2) at flow rate of 0.5 mL/min. The black bar represents relaxing active fractions on the starfish DRM.
$Fig. 13. Reverse-phase HPLC profile of the active fraction in Fig. 12. The active fraction in Fig. 12 was loaded onto Hypersil-BDS C18 (2 × 125 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 0.5 mL/min. The black bar represents relaxing active peak on the starfish DRM.$ 표 Fig. 13. Reverse-phase HPLC profile of the active fraction in Fig. 12. The active fraction in Fig. 12 was loaded onto Hypersil-BDS C18 (2 × 125 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 0.5 mL/min. The black bar represents relaxing active peak on the starfish DRM.
$Fig. 14 Anion-exchange HPLC profile of the active fraction in Fig. 13. The active fraction in Fig. 13 was pooled and loaded onto DEAE-5PW (7.5 × 75 mm) column and eluted with a linear gradient of 1.0 M NaCl (dotted line) in 10 mM Tris-HCl buffer (pH 9.2) at flow rate of 0.5 mL/min. The black bar represents relaxing active fractions on the starfish DRM.$ 표 Fig. 14 Anion-exchange HPLC profile of the active fraction in Fig. 13. The active fraction in Fig. 13 was pooled and loaded onto DEAE-5PW (7.5 × 75 mm) column and eluted with a linear gradient of 1.0 M NaCl (dotted line) in 10 mM Tris-HCl buffer (pH 9.2) at flow rate of 0.5 mL/min. The black bar represents relaxing active fractions on the starfish DRM.
$Fig. 15. Reverse-phase HPLC chromatography of the active fraction in Fig. 14. The active fraction in Fig. 14 was pooled and loaded onto Hypersil BDS C18 (2 × 125 mm) column and eluted with isocratically 23 % CH3CN in 0.1 % TFA at flow rate of 0.5 mL/min. The black bar represents relaxing active fractions on the starfish DRM.$ 표 Fig. 15. Reverse-phase HPLC chromatography of the active fraction in Fig. 14. The active fraction in Fig. 14 was pooled and loaded onto Hypersil BDS C18 (2 × 125 mm) column and eluted with isocratically 23 % CH3CN in 0.1 % TFA at flow rate of 0.5 mL/min. The black bar represents relaxing active fractions on the starfish DRM.
$Fig. 16. Final purification of the active fraction in Fig. 15. The active fraction in Fig. 15 was loaded onto a Superdex Peptide HR 10/30 (10 × 300 mm) and eluted with isocratically 30 % CH3CN in 0.1 % TFA at flow rate of 0.5 mL/min (A). The down arrow represents the sample applied to the starfish DRM (B). The molecular weight of single peak (down arrow) of Fig. 16A was determined by MALDI-TOF Mass spectra (C).$ 표 Fig. 16. Final purification of the active fraction in Fig. 15. The active fraction in Fig. 15 was loaded onto a Superdex Peptide HR 10/30 (10 × 300 mm) and eluted with isocratically 30 % CH3CN in 0.1 % TFA at flow rate of 0.5 mL/min (A). The down arrow represents the sample applied to the starfish DRM (B). The molecular weight of single peak (down arrow) of Fig. 16A was determined by MALDI-TOF Mass spectra (C).
$Fig. 17. Anion exchange HPLC profile of the active fraction B-I in Fig. 11. The active fraction B-I in Fig. 11 was loaded onto DEAE-5PW (7.5 × 75 mm) column and eluted with a linear gradient of 1.0 M NaCl (dotted line) in 10 mM Tris-HCl buffer (pH 9.2) at flow rate of 0.5 mL/min. The black bar represents relaxing active fractions on the starfish DRM.$ 표 Fig. 17. Anion exchange HPLC profile of the active fraction B-I in Fig. 11. The active fraction B-I in Fig. 11 was loaded onto DEAE-5PW (7.5 × 75 mm) column and eluted with a linear gradient of 1.0 M NaCl (dotted line) in 10 mM Tris-HCl buffer (pH 9.2) at flow rate of 0.5 mL/min. The black bar represents relaxing active fractions on the starfish DRM.
$Fig. 18. Reverse-Phase HPLC profile of the active fraction in Fig. 17. The active fractions in Fig. 17 were pooled and loaded onto Capcellpak C18 (4.6 × 250 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 1.0 mL/min. The black bar represents relaxing active peak on the starfish DRM.$ 표 Fig. 18. Reverse-Phase HPLC profile of the active fraction in Fig. 17. The active fractions in Fig. 17 were pooled and loaded onto Capcellpak C18 (4.6 × 250 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 1.0 mL/min. The black bar represents relaxing active peak on the starfish DRM.
$Fig. 19. Reverse-Phase HPLC profile of the active fraction in Fig. 18. The active fraction in Fig. 18 was pooled and loaded on to Hypersil-BDS C18 (2 × 125 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 0.5 mL/min. The black bar represents relaxing active peak on the starfish DRM.$ 표 Fig. 19. Reverse-Phase HPLC profile of the active fraction in Fig. 18. The active fraction in Fig. 18 was pooled and loaded on to Hypersil-BDS C18 (2 × 125 mm) column and eluted with a linear gradient of CH3CN (dotted line) in 0.1 % TFA at flow rate of 0.5 mL/min. The black bar represents relaxing active peak on the starfish DRM.
$Fig. 20. Final purification of the active fraction in Fig. 19. The active fraction was loaded onto a Hypersil BDS C18 (2 × 125 mm) and eluted with isocratically 20 % CH3CN in 0.1 % TFA at flow rate of 0.5 mL/min (A), and the bioassay with the starfish DRM (B). The molecular weight of single peak (down arrow) of Fig. 6A was determined by MALDI-TOF Mass spectra (C).$ 표 Fig. 20. Final purification of the active fraction in Fig. 19. The active fraction was loaded onto a Hypersil BDS C18 (2 × 125 mm) and eluted with isocratically 20 % CH3CN in 0.1 % TFA at flow rate of 0.5 mL/min (A), and the bioassay with the starfish DRM (B). The molecular weight of single peak (down arrow) of Fig. 6A was determined by MALDI-TOF Mass spectra (C).
$Fig. 21. The 1st purification of SFM-I on a Vydac C4 column. RM60 was eluted with a linear gradient of 10 ~ 10% B (10 min) → 65% B (40 min) CH3CN in 0.1% TFA (pH 2.2) at a flow rate of 1.0 ml/min. The down arrow shows the fraction with antimicrobial activity against B. subtilis KCTC 1021.$ 표 Fig. 21. The 1st purification of SFM-I on a Vydac C4 column. RM60 was eluted with a linear gradient of 10 ~ 10% B (10 min) → 65% B (40 min) CH3CN in 0.1% TFA (pH 2.2) at a flow rate of 1.0 ml/min. The down arrow shows the fraction with antimicrobial activity against B. subtilis KCTC 1021.
$Fig. 22. The 2nd purification of SFM-I on a Capcell-Pak C18 column. Active fraction was eluted with a linear gradient of 10 ~ 10 % B (10 min) → 60 % B (50 min) CH3CN in 0.1 % TFA (pH 2.2) at a flow rate of 1.0 ml/min. The down arrow shows the fraction with antimicrobial activity against B. subtilis KCTC 1021.$ 표 Fig. 22. The 2nd purification of SFM-I on a Capcell-Pak C18 column. Active fraction was eluted with a linear gradient of 10 ~ 10 % B (10 min) → 60 % B (50 min) CH3CN in 0.1 % TFA (pH 2.2) at a flow rate of 1.0 ml/min. The down arrow shows the fraction with antimicrobial activity against B. subtilis KCTC 1021.
$Fig. 23. The final purification of SFM-I on a Capcell-Pak C18 column. Active fraction was eluted with a linear gradient of 10% ~ 10% B (10 min) → 60% B (50 min) CH3CN in 0.1 % TFA (pH 2.2) at a flow rate of 1.0 ml/min. The fraction shows antimicrobial activity against B. subtilis KCTC 1021.$ 표 Fig. 23. The final purification of SFM-I on a Capcell-Pak C18 column. Active fraction was eluted with a linear gradient of 10% ~ 10% B (10 min) → 60% B (50 min) CH3CN in 0.1 % TFA (pH 2.2) at a flow rate of 1.0 ml/min. The fraction shows antimicrobial activity against B. subtilis KCTC 1021.
표 Fig. 24. A comparison between HPLC profiles of the native SF-CT (N) and synthetic SF-CT (S). N and S were injected to a C18 reverse-phase (μ- Bondapak C18 column) column with a linear gradient CH3CN concentrations from 0 to 60 % in 0.1 % TFA for 30 min at a flow rate of 1 ml/min. N+S represents a mixture of the native and synthetic peptide.
표 Fig. 25. A comparison between HPLC profiles of the native SF-CNP (N) and synthetic SF-CNP (S). N and S were injected to a C18 reverse-phase (μ- Bondapak C18 column) column with a linear gradient CH3CN concentrations from 0 to 60 % in 0.1 % TFA for 30 min at a flow rate of 1 ml/min. N+S represents a mixture of the native and synthetic peptide.
표 Fig. 26. Concentration response curves to SF-CT and SF-CNP (n=5) induced relaxation in starfish DRM : SF-CT (●) and SF-CNP (○). Relaxing effects expressed as % the maximal response to ACh, 1×10-5 M.
표 Fig. 27. Concentration response curves to SF-CT, H-CT and S-CT (n=5) induced relaxation in starfish DRM : SF-CT (●), H-CT (○) and S-CT(▼). Relaxing effects expressed as % the maximal response to ACh, 1×10-5 M.
표 Fig. 28. (A) Time dependence analysis of the effect on MEK1/2 and ERK1/2 phosphorylation in MDA-MB-231 cells were treated with 250 nM of SF-CT. (B) Human calcitonin supresses phosphorylation of ERK1/2 in MDA-MB-231 cells which were treated with 30 min.
표 Fig 29. Time dependence analysis of the effect on Ser338-C-Raf/Ser259-Craf and Ser445-B-Raf phosphorylation in MDA-MB-231cells which were treated with 250 nM of SF-CT.
표 Fig 30. Time dependence analysis of the effect on Thr638/641PKCα/βⅡ phosphorylation in MDA-MB-231 cells which were treated with 250 nM of SF-CT.
표 Fig. 31. MDA-MB-231 cells were incubated with SF-CT 100 nM (0.1㎕/㎖), 250 nM (0.25 ㎕/㎖), 500 nM (0.5 ㎕/㎖), added to the cells and incubation for 12hr in 37 ℃, 5% CO2 condition
표 Fig. 32. Measurement of intracellular cAMP concentration in MDA-MB-231 cells were incubated with SF-CT 250 nM (0.25㎕/㎖), 500 nM (0.5㎕/㎖) added to the cells and incubation for 30 min in 37 ℃, 5 % CO2 condition
표 Fig. 33. Concentration response curves to SF-CT analogues (n=5) induced relaxation in starfish DRM: 1DES-SF-CT (●), 1DES2-SF-CT (○), 1DES3 -SF-CT(▼) and 1DES4-SF-CT (△). Relaxing effects expressed as % the maximal response to ACh, 1×10-5 M.
표 Fig. 34 Concentration response curves to SF-CNP analogues (n=5) induced relaxation in starfish DRM: 1DES-SF-CNP (●), 1DES2-SF-CNP(○) and 1DES3-[A4,20]-SF-CNP (▼). Relaxing effects expressed as % the maximal response to ACh, 1×10-5 M.
표 Fig. 35. cAMP activity. Measurement of intracellular cAMP concentration in HEK 293 cells were incubated with 500 nM SF-CT and SF-CT analogues added to the cells and incubation for 30 min in 37 ℃, 5 % CO2 condition
표 Fig. 36. 3’ RACE PCR products from Asterina pectinifera cDNA (A) and sequencing result (B): (A) Lane 1: Bioneer 100bp plus DNA ladder, Lane 2: SF-CT-1 primer -related PCR products from Asterina pectinifera cDNA, Lane 3: SF-CT-2 primerrelated PCR products from Asterina pectinifera cDNA. (B) The sequencing result was 569bp including 446bp as a 3’UTR. SF-CT 5’primers were underlined.
표 Fig. 37. 5’ RACE PCR products from Asterina pectinifera cDNA (A) and sequencing result (B): (A) Lane 1: Bioneer 100bp plus DNA ladder, Lane 2: SF-CT_5'-1 primer -related PCR products from full length Asterina pectinifera cDNA, Lane 3: SF-CT_5'-2 primer-related PCR products from full length Asterina pectinifera cDNA. (B) The sequencing result was 461bp including 117bp as a 5’ UTR. SF-CT was indicated by box and 5’primer underlined.
표 Fig. 38. Nucleotide sequence of SF-CT cDNA with the amino acid sequence for the prepropeptide: signal peptide underlined and SF-CT boxed. Arrows indicate to the cleavage site by dibasic peptidase.
표 Fig. 39. Diagram of SF-CT cDNA full sequence: KR indicates the cleavage site by dibasic peptidase.
표 Fig. 40. The N-terminal sequences of some eukaryotic secretory preproteins
표 Fig. 41. SF-CT tissue type expression: lane 1, stomach; lane 2, liver; lane 3, gonad; lane 4, dorsal retractor muscle (DRM); lane 5, tube foot. Expression of a gene encoding the β-actin was used as a control.
표 Fig. 42. 3’RACE PCR products from Asterina pectinifera cDNA (A) and sequencing result (B): (A) Lane 1: Bioneer 25/100bp DNA ladder, Lane 2: SF-CNP-1 primerrelated PCR products from Asterina pectinifera cDNA, Lane 3: SF-CNP-2 primerrelated PCR products from Asterina pectinifera cDNA, Lane 4: SF-CNP-3 primerrelated PCR products from Asterina pectinifera cDNA. (B) The sequencing result was 277bp including 199bp as a 3’UTR. SF-CNP 5’primers were underlined.
표 Fig. 43. 5’RACE PCR products from Asterina pectinifera cDNA (A) and sequencing result (B)
표 Fig. 44. Nucleotide sequence of SF-CNP cDNA with the amino acid sequence for the prepropeptide: signal peptide underlined and SF-CNP boxed. Arrows indicate to the cleavage site by dibasic peptidase.
표 Fig. 45. Diagram of SF-CNP DNA full sequence: KR and RR indicate the cleavage site by dibasic peptidase.
표 Fig. 46. SF-CNP tissue type expression: lane 1, stomach; lane 2, liver; lane 3, gonad; lane 4, dorsal retractor muscle (DRM); lane 5, tube foot. Expression of a gene encoding the β-actin was used as a control.
표 Fig. 47. 불가사리 먹이 선택성 시험 및 구제 시험 조업지역
표 1항차 먹이별 불가사리 어획률 (해상시험)
표 3항차 먹이별 불가사리 어획률 (해상시험)
표 Fig. 48. 불가사리 구제를 위한 통발 종류
표 Fig. 49. 불가사리 구제 어구개발 기초시험을 위한 수조 모형
표 통발 종류별 불가사리 포획량 (실내 수조시험)
표 제3차 통발별 불가사리 포획시험(해상시험)
표 3회 합계 통발별 불가사리 포획율(해상시험)

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