Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas
In the previous papers^(1.2), we investigated the effects of ACE inhibitory activities of phosphopeptides of P-1 and C-2 which were obtained from edible oyster by proteolytic hydrolyzation. In this investigation, the ACE inhibitory phosphopeptides of T-1 was further purified by ultrafiltration and S...
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ftnagasakiuniv:oai:nagasaki-u.repo.nii.ac.jp:00023822 2023-05-15T15:58:53+02:00 Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas Tamari Masato Kai Masae Kanda Hiroko 2000-06 http://hdl.handle.net/10069/6087 https://nagasaki-u.repo.nii.ac.jp/?action=repository_uri&item_id=23822 https://nagasaki-u.repo.nii.ac.jp/?action=repository_action_common_download&item_id=23822&item_no=1&attribute_id=18&file_no=1 en eng https://nagasaki-u.repo.nii.ac.jp/?action=repository_uri&item_id=23822 http://hdl.handle.net/10069/6087 長崎大学教育学部紀要. 自然科学, 63, 39-48(2000-06) 13451359 AA11330079 https://nagasaki-u.repo.nii.ac.jp/?action=repository_action_common_download&item_id=23822&item_no=1&attribute_id=18&file_no=1 長崎大学教育学部紀要. 教育科学. vol.67, p.21-28; 2004@@@長崎大学教育学部紀要. 自然科学. vol.63, p.39-48; 2000 Departmental Bulletin Paper 2000 ftnagasakiuniv 2022-12-02T01:21:17Z In the previous papers^(1.2), we investigated the effects of ACE inhibitory activities of phosphopeptides of P-1 and C-2 which were obtained from edible oyster by proteolytic hydrolyzation. In this investigation, the ACE inhibitory phosphopeptides of T-1 was further purified by ultrafiltration and Sephadex G-15 column chromatography. ACE inhibitory activity was fractionated into three major phosphopeptides fractions of T-1-1,T-1-2 and T-1-3 in the pepsin hydrolyzates of the T-1 by gel filtration rechromatography on Sephadex G-15. The inhibition of ACE of the three kinds of phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) was analyzed in vitro. The IC_<50> values of T-1-1,T-1-2 and T-1-3 of phosphopeptides for ACE were 0.159,0.095 and 0.140 mg protein/ml, respectively. The T-1-2 fraction had the most potent inyhibitory activity and showed 0.095 mg protein/ml inhibition against ACE at IC_<50> value. It has been demonstrated that the T-1-1,T-1-2 and T-1-3 contained about 33.3%, 3.01% and 27.12% as phosphonate-phosphorus of total phosphorus. The amino acid compositions of the phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) were characterized by relatively high percentage for Tyr, Ser, Arg, Ala, Asp and Phe. When the ACE inhibitory phosphopeptides were analyzed by thin layer chromatography, some ninhydrine-positive spots were observed. These results suggest that the phosphopeptides are a mixture of several phosphopeptides. Report Crassostrea gigas NAOSITE: Nagasaki University Academic Output SITE |
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English |
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In the previous papers^(1.2), we investigated the effects of ACE inhibitory activities of phosphopeptides of P-1 and C-2 which were obtained from edible oyster by proteolytic hydrolyzation. In this investigation, the ACE inhibitory phosphopeptides of T-1 was further purified by ultrafiltration and Sephadex G-15 column chromatography. ACE inhibitory activity was fractionated into three major phosphopeptides fractions of T-1-1,T-1-2 and T-1-3 in the pepsin hydrolyzates of the T-1 by gel filtration rechromatography on Sephadex G-15. The inhibition of ACE of the three kinds of phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) was analyzed in vitro. The IC_<50> values of T-1-1,T-1-2 and T-1-3 of phosphopeptides for ACE were 0.159,0.095 and 0.140 mg protein/ml, respectively. The T-1-2 fraction had the most potent inyhibitory activity and showed 0.095 mg protein/ml inhibition against ACE at IC_<50> value. It has been demonstrated that the T-1-1,T-1-2 and T-1-3 contained about 33.3%, 3.01% and 27.12% as phosphonate-phosphorus of total phosphorus. The amino acid compositions of the phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) were characterized by relatively high percentage for Tyr, Ser, Arg, Ala, Asp and Phe. When the ACE inhibitory phosphopeptides were analyzed by thin layer chromatography, some ninhydrine-positive spots were observed. These results suggest that the phosphopeptides are a mixture of several phosphopeptides. |
format |
Report |
author |
Tamari Masato Kai Masae Kanda Hiroko |
spellingShingle |
Tamari Masato Kai Masae Kanda Hiroko Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas |
author_facet |
Tamari Masato Kai Masae Kanda Hiroko |
author_sort |
Tamari Masato |
title |
Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas |
title_short |
Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas |
title_full |
Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas |
title_fullStr |
Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas |
title_full_unstemmed |
Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas |
title_sort |
inhibitory activity of angiotensin 1-converting enzyme of phosphopeptides obtained from proteolytic hydrolyzates of oyster, crassostrea gigas |
publishDate |
2000 |
url |
http://hdl.handle.net/10069/6087 https://nagasaki-u.repo.nii.ac.jp/?action=repository_uri&item_id=23822 https://nagasaki-u.repo.nii.ac.jp/?action=repository_action_common_download&item_id=23822&item_no=1&attribute_id=18&file_no=1 |
genre |
Crassostrea gigas |
genre_facet |
Crassostrea gigas |
op_relation |
https://nagasaki-u.repo.nii.ac.jp/?action=repository_uri&item_id=23822 http://hdl.handle.net/10069/6087 長崎大学教育学部紀要. 自然科学, 63, 39-48(2000-06) 13451359 AA11330079 https://nagasaki-u.repo.nii.ac.jp/?action=repository_action_common_download&item_id=23822&item_no=1&attribute_id=18&file_no=1 長崎大学教育学部紀要. 教育科学. vol.67, p.21-28; 2004@@@長崎大学教育学部紀要. 自然科学. vol.63, p.39-48; 2000 |
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1766394663548223488 |