Fig. 1. The renin-angiotensin system and kallikrein-kinin system=2,30,1

Fig. 2. Schematic diagram of structural domains of angiotensin I converting enzyme=3,31,1

Fig. 3. The sources and cellular responses to reactive oxygen species=6,34,1

Fig. 4. Schematic procedure for the extraction of crude enzyme from Tuna intestine=11,39,1

Fig. 5. Proteinolytic activities of TICE on synthetic substrates=31,59,1

Fig. 6. Comparison of proteolytic activity between commercial enzymes and TICE. substrate(Yellowfin sole frame protein)=33,61,1

Fig. 7. Effect of pH on the hydrolysis of Yellowfin sole frame protein by TICE=34,62,1

Fig. 8. Effect of temperature on the hydrolysis of Yellowfin sole frame protein by TICE=36,64,1

Fig. 9. Effect of substrate concentration on the hydrolysis of Yellowfin sole frame protein by TICE=37,65,1

Fig. 10. Effect of substrate／enzyme ratio on the hydrolysis of Yellowfin sole frame protein by TICE=39,67,1

Fig. 11. Effect of incubation time on the hydrolysis of Yellowfin sole frame protein by TICE=40,68,1

Fig. 12. Effects of antioxidative activity of hydrolysates of various enzyme from Yellowfin sole protein in linoleic acid autoxidation system measured by the ferric thiocyanate method=43,71,1

Fig. 13. Effects of ACE inhibitory activity of hydrolysates of various enzymes from Yellowfin sole frame protein=44,72,1

Fig. 14. Procedures for the purification and characterization of antioxidative peptides from Yellowfin sole frame protein=45,73,1

Fig. 15. Molecular weight distribution profiles of YFP I,II,III,IV and V on HPLC with GPC column=48,76,1

Fig. 16. Antioxidative activity of hydrolysates of TICE + pepsin from Yellowfin sole protein in linoleic acid autoxidation system measured by the ferric thiocyanate method=50,78,1

Fig. 17. Radical scavenging activity of hydrolysates of TICE + pepsin enzyme from Yellow fin sole protein on DPPH radical=51,79,1

Fig. 18. Antioxidative activity of YFP I at various concentration in linoleic acid autoxidation system by the ferric thiocyanate method=54,82,1

Fig. 19. Radical scavenging activity of YFP I at various concentration on DPPH radical=55,83,1

Fig. 20. Synergistic effects of α-tocopherol and hydrolysates of TICE + pepsin from Yellowfin sole protein in linoleic acid autoxidation system measured by the ferric thiocranate method=56,84,1

Fig. 21. Separation of YFP I by SP-Sephadex C-25 column chromatography (lower panel) and antioxidative activities (upper panel) of the fractions (I,II and III)=59,87,1

Fig. 22. Purification of fraction III on Sephadex G-75 gel chromatography (lower panel) and antioxidative activities(upper panel) of the fractions(III-1)=60,88,1

Fig. 23. Reverse-phase HPLC pattern on a Primary 10 C-18 column of active fraction III eluted on the Sephadex G-75 gel chromatography (lower panel) and antioxidative activities (upper panel) of the fractions (III-1-1,III-1-2,III-1-3,III-1-4)=61,89,1

Fig. 24. Reverse-phase HPLC pattern on a Primary 10 C-18 column of active fraction III-1-1 eluted on the HPLC (lower panel) and antioxidative activities (upper panel) of the fractions (III-1-1a,III-1-1b)=62,90,1

Fig. 25. SDS-PACE of the purified enzymatic hydrolysates of Yellowfin sole frame protein on 12.5% gels under denaturing condition=64,92,1

Fig. 26. Cytotoxicity of antioxidative peptide from Yellowfin sole frame protein (YFP) on cultured normal human liver cells=68,96,1

Fig. 27. Effect of t-BHP concentration on cell killing of cultured cells without and with antioxidative peptide from Yellowfin sole frame protein(YFP)=69,97,1

Fig. 28. Effect of antioxidative peptide from Yellowfin sole frame protein (YFP) on lipid peroxidation induced by t-BHP treatment in cultured liver cells=70,98,1

Fig. 29. Effect of antioxidatve peptide from Yellowfin sole frame protein (YFP) on catalase activity induced by t-BHP treatment in cultured liver cells=71,99,1

Fig. 30. Effect of antioxidative peptide from Yellowfin sole frame protein (YFP) on superoxide dismutase activity induced by t-BHP treatment in cultured liver cells=72,100,1

Fig. 31. Effect of antioxidative peptide from Yellowfin sole frame protein(YFP) on glutathione peroxidase activity induced by t-BHP treatment in cultured liver cells=73,101,1

Fig. 32. Effect of antioxidative peptide from Yellowfin sole protein (YFP) on glutathione S-transferase activity induced by t-BHP treatment in cultured liver cells=74,102,1

Fig. 33. Procedures for the purification and characterization of ACE inhibitory peptides from Yellowfin sole Came protein=76,104,1

Fig. 34. Distribution of ACE inhibitory peptides hydrolyzed from Yellowfin sole frame protein by ultrafiltration membrane (1-3 kDa)=78,106,1

Fig. 35. Purification of ACE inhibitory peptides from yellowfin sole frame protein,Ion exchange chromatogram on SP-Sephadex C-25=81,109,1

Fig. 36. Purification of ACE inhibitory peptides from yellowfin sole frame protein=83,111,1

Fig. 37. Purification of ACE inhibitory peptides from yellowfin sole frame protein=85,113,1

Fig. 38. Purification of ACE inhibitory peptides from yellowfin sole frame protein=87,115,1

Fig. 39. Identification of molecular weight and purity of ACE inhibitory peptide from Yellowfin frame hydrolysate=92,120,1

Fig. 40. Change in systolic blood pressure (SBP) of SHR by administering ACE inhibitory peptide=93,121,1

Fig. 41. Binding interactions substrate (Leu-Gly-Pro) based on active sitemodel of ACE by Ondetti and Cushman (1984)=94,122,1

Fig. 42. Procedures for the purification and characterization of antioxidative peptides from hoki skin gelatin=98,126,1

Fig. 43. Degree of hydrolysis of hoki skin gelatin by various enzymes=99,127,1

Fig. 44. Effects of antioxidative activity of hydrolysates from hoki skin gelatin by various enzymes in linoleic acid autoxidation system measured by the ferric thiocyanate method=103,131,1

Fig. 45. Effects of ACE inhibitory activity of hydrolysates from hoki skin gelatin by various enzymes=104,132,1

Fig. 46. Antioxidative activity of hydrolysates of TICE + α-chymotrypsin from hoki skin gelatin in linoleic acid autoxidation system measured by the ferric thiocyanate method=105,133,1

Fig. 47. Synergistic effects of α-tocopherol and hydrolysates of TICE + α-chymotrypsin from hoki skin gelatin in linoleic acid autoxidation system measured by the ferric thiocyanate method=106,134,1

Fig. 48. Profile of cation exchange chromatography of HSG I on SP-Sephadex C-25 column=108,136,1

Fig. 49. Pattern of Gel chromatography on Sephadex G-50=109,137,1

Fig. 50. Reverse-phase HPLC pattern on a Primary 10 C-18 column of active fraction G-3 eluted on the Sephadex G-75 gel chromatography=110,138,1

Fig. 51. Antioxidative activity of P-HSG in linoleic acid autoxidation system measured by the ferric thiocyanate method=111,139,1

Fig. 52. Identification of molecular weight and purity of antioxidative peptide from hoki skin gelatin=113,141,1

Fig. 53. Cytotoxicity of antioxidative peptide from hoki skin gelatin on cultured normal human liver cells=115,143,1

Fig. 54. Effect of t-BHP concentration on cell killing of cultured cells without and with antioxidative peptide from hoki skin gelatin (HSG)=116,144,1

Fig. 55. Effect of antioxidative peptide from hoki skin on lipid peroxidation induced by t-BHP in cultured liver cells=117,145,1

Fig. 56. Effect of antioxidative peptide from hoki skin gelatin (HSC) on catalase activity induced by t-BHP treatment in liver cells=119,147,1

Fig. 57 Effect of antioxidative peptide from hoki skin gelatin (HSC) on superoxide dismutase activity induced by t-BHP treatment in cultured liver cells=120,148,1

Fig. 58. Effect of antioxidative peptide from hoki skin gelatin (HSC) on glutathione peroxidase activity induced by t-BHP treatment in cultured liver cells=121,149,1

Fig. 59. Effect of antioxidative peptide from hoki skin gelatin (HSC) on glutathione S-transferase activity induced by t-BHP treatment in cultured liver cells=122,150,1

Fig. 1. Gel filtration chromatography of fermented mussel saucse (FMS) on the Sephadex G-75 column and the ACE inhibitory activity=146,174,1

Fig. 2. Ion-exchange chromatography of active fraction B on the SP-Sephadex C-25 column and ACE inhibitory activity=147,175,1

Fig. 3. Reversed-phase HPLC pattern on a Nucleosil 100-7 ODS C18(이미지참조) column of active fraction BIII=148,176,1

Fig. 4. Rechromatography of fraction BIIIb pooled on HPLC on a Nucleosil 100-7 ODS C18(이미지참조) column=149,177,1

Fig. 5. Determination of molecular weight of purified peptide on HPLC with GPC column=150,178,1

Fig. 6,Change in systolic blood pressure (SBP) of SHR by administering ACE inhibitory peptide=152,180,1

Fig. 7. Purification of anticancer peptide from mussel using liquid chromatographies=154,182,4

Fig. 8. Cytotoxicity of a fermented mussel on cultured normal human liver cells (Chang cell)=158,186,1

Fig. 9. Antitumor activity of fermented mussel on cultured various cancer cells=159,187,1