食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるACEの阻害活性

In this investigation, the ACE inhibitory phosphopeptides of P-1 and C-2 were further purified by ultrafiltration and by Sephadex G-15 chromatography. ACE inhibitory activity was fractionated into three major phosphopeptides fractions of P-1-1,P-1-2 and P-1-3 in the pepsin hydrolyzates of the P-1,an...

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Main Authors: 玉利 正人, 神田 浩子
Format: Report
Language:English
Published: 2000
Subjects:
Online Access:http://hdl.handle.net/10069/6081
https://nagasaki-u.repo.nii.ac.jp/?action=repository_uri&item_id=23816
https://nagasaki-u.repo.nii.ac.jp/?action=repository_action_common_download&item_id=23816&item_no=1&attribute_id=18&file_no=1
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spelling ftnagasakiuniv:oai:nagasaki-u.repo.nii.ac.jp:00023816 2023-05-15T15:59:08+02:00 食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるACEの阻害活性 Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster,Crassostrea gigas 玉利 正人 神田 浩子 2000-03 http://hdl.handle.net/10069/6081 https://nagasaki-u.repo.nii.ac.jp/?action=repository_uri&item_id=23816 https://nagasaki-u.repo.nii.ac.jp/?action=repository_action_common_download&item_id=23816&item_no=1&attribute_id=18&file_no=1 en eng https://nagasaki-u.repo.nii.ac.jp/?action=repository_uri&item_id=23816 http://hdl.handle.net/10069/6081 長崎大学教育学部紀要. 自然科学, 62, 29-40(2000-03) 13451359 AA11330079 https://nagasaki-u.repo.nii.ac.jp/?action=repository_action_common_download&item_id=23816&item_no=1&attribute_id=18&file_no=1 長崎大学教育学部紀要. 教育科学. vol.66, p.25-39; 2004@@@長崎大学教育学部紀要. 自然科学. vol.62, p.29-40; 2000 Departmental Bulletin Paper 2000 ftnagasakiuniv 2022-12-02T01:21:17Z In this investigation, the ACE inhibitory phosphopeptides of P-1 and C-2 were further purified by ultrafiltration and by Sephadex G-15 chromatography. ACE inhibitory activity was fractionated into three major phosphopeptides fractions of P-1-1,P-1-2 and P-1-3 in the pepsin hydrolyzates of the P-1,and into fractions of C-2-1,C-2-2 and C-2-3 in the pepsin hydrolyzates of the C-2 by gel filtration rechromatography on Sephadex G-15,respectively. The inhibition of ACE of the six kinds of phosphopeptides fractions (P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3) was analyzed in vitro. The IC_<50> values of P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3 of phosphopeptides for ACE were 1.11,0.04,0.05,1.04,0.72 and 0.06mg protein/ml, respectively. The P-1-2 fraction had the most inhibitory activity and showed 0.04mg protein/ml inhibition against ACE at IC_<50> value. It has been demonstrated that the P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3 contained about 23.2%, 4.4%, 28.1%, 2.0%, 3.8% and 1.6% as phosphonate-phosphorus of total phosphorus. The amino acid compositions of the phosphopeptides fractions (P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3) were characterized by relatively high percentage for Glu, Asp, Gly, Ala, Val, Leu, Tyr, Phe, Lys and Arg. 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. The results above, the Sephadex G-15 gel filtration patterns of the active fraction obtained from the Sephadex G-50 column chromatography indicated that the molecular weight of the phosphopeptide was about 200 ∿ 1000. Report Crassostrea gigas NAOSITE: Nagasaki University Academic Output SITE
institution Open Polar
collection NAOSITE: Nagasaki University Academic Output SITE
op_collection_id ftnagasakiuniv
language English
description In this investigation, the ACE inhibitory phosphopeptides of P-1 and C-2 were further purified by ultrafiltration and by Sephadex G-15 chromatography. ACE inhibitory activity was fractionated into three major phosphopeptides fractions of P-1-1,P-1-2 and P-1-3 in the pepsin hydrolyzates of the P-1,and into fractions of C-2-1,C-2-2 and C-2-3 in the pepsin hydrolyzates of the C-2 by gel filtration rechromatography on Sephadex G-15,respectively. The inhibition of ACE of the six kinds of phosphopeptides fractions (P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3) was analyzed in vitro. The IC_<50> values of P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3 of phosphopeptides for ACE were 1.11,0.04,0.05,1.04,0.72 and 0.06mg protein/ml, respectively. The P-1-2 fraction had the most inhibitory activity and showed 0.04mg protein/ml inhibition against ACE at IC_<50> value. It has been demonstrated that the P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3 contained about 23.2%, 4.4%, 28.1%, 2.0%, 3.8% and 1.6% as phosphonate-phosphorus of total phosphorus. The amino acid compositions of the phosphopeptides fractions (P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3) were characterized by relatively high percentage for Glu, Asp, Gly, Ala, Val, Leu, Tyr, Phe, Lys and Arg. 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. The results above, the Sephadex G-15 gel filtration patterns of the active fraction obtained from the Sephadex G-50 column chromatography indicated that the molecular weight of the phosphopeptide was about 200 ∿ 1000.
format Report
author 玉利 正人
神田 浩子
spellingShingle 玉利 正人
神田 浩子
食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるACEの阻害活性
author_facet 玉利 正人
神田 浩子
author_sort 玉利 正人
title 食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるACEの阻害活性
title_short 食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるACEの阻害活性
title_full 食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるACEの阻害活性
title_fullStr 食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるACEの阻害活性
title_full_unstemmed 食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるACEの阻害活性
title_sort 食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるaceの阻害活性
publishDate 2000
url http://hdl.handle.net/10069/6081
https://nagasaki-u.repo.nii.ac.jp/?action=repository_uri&item_id=23816
https://nagasaki-u.repo.nii.ac.jp/?action=repository_action_common_download&item_id=23816&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=23816
http://hdl.handle.net/10069/6081
長崎大学教育学部紀要. 自然科学, 62, 29-40(2000-03)
13451359
AA11330079
https://nagasaki-u.repo.nii.ac.jp/?action=repository_action_common_download&item_id=23816&item_no=1&attribute_id=18&file_no=1
長崎大学教育学部紀要. 教育科学. vol.66, p.25-39; 2004@@@長崎大学教育学部紀要. 自然科学. vol.62, p.29-40; 2000
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