Characterization of an Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Peptide from the Edible Mushroom Hypsizygus marmoreus
Hypertension is one of the very serious diseases and, recently, hypertensive patient longevity has been increased significantly. Therefore, the development of new antihypertensive drugs or bioactive compounds is very important to remedy or prevent hypertension. The antihypertensive angiotensin I-con...
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| Veröffentlicht in: | BioMed research international 2013-01, Vol.2013 (2013), p.1-6 |
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| creator | Seo, Geon-Sik Kim, Min-Kyung Bolormaa, Zanabaatar Kim, Young-Hun Kang, Min-Gu Lee, Jong-Soo |
| description | Hypertension is one of the very serious diseases and, recently, hypertensive patient longevity has been increased significantly. Therefore, the development of new antihypertensive drugs or bioactive compounds is very important to remedy or prevent hypertension. The antihypertensive angiotensin I-converting enzyme (ACE) inhibitor in water extracts from the brown-cultivar-fruiting-body of Hypsizygus marmoreus was purified with ultrafiltration, C18 solid phase extraction chromatography and reverse-phase HPLC, and the purified ACE inhibitor with inhibitory activity of IC50 value of 0.19 mg/mL was obtained. The purified ACE inhibitor was found to be a new oligopeptide with the sequence LSMGSASLSP. Its molecular weight was estimated to be 567.3 Da and the water extracts containing ACE inhibitor from Hypsizygus marmoreus showed a clear antihypertensive action a spontaneously hypertensive rat. |
| doi_str_mv | 10.1155/2013/283964 |
| format | Article |
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Therefore, the development of new antihypertensive drugs or bioactive compounds is very important to remedy or prevent hypertension. The antihypertensive angiotensin I-converting enzyme (ACE) inhibitor in water extracts from the brown-cultivar-fruiting-body of Hypsizygus marmoreus was purified with ultrafiltration, C18 solid phase extraction chromatography and reverse-phase HPLC, and the purified ACE inhibitor with inhibitory activity of IC50 value of 0.19 mg/mL was obtained. The purified ACE inhibitor was found to be a new oligopeptide with the sequence LSMGSASLSP. Its molecular weight was estimated to be 567.3 Da and the water extracts containing ACE inhibitor from Hypsizygus marmoreus showed a clear antihypertensive action a spontaneously hypertensive rat.</description><identifier>ISSN: 2314-6133</identifier><identifier>EISSN: 2314-6141</identifier><identifier>DOI: 10.1155/2013/283964</identifier><identifier>PMID: 24380081</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Publishing Corporation</publisher><subject>Agaricales - enzymology ; Angiotensin converting enzyme ; Angiotensin-Converting Enzyme Inhibitors - administration & dosage ; Angiotensin-Converting Enzyme Inhibitors - chemistry ; Angiotensin-Converting Enzyme Inhibitors - isolation & purification ; Animals ; Antihypertensive Agents - administration & dosage ; Antihypertensive Agents - chemistry ; Basidiomycota ; Biological products ; Blood Pressure - drug effects ; Care and treatment ; Chromatography, High Pressure Liquid ; Health aspects ; Humans ; Hypertension ; Hypertension - drug therapy ; Hypertension - pathology ; Identification and classification ; Peptides - administration & dosage ; Peptides - chemistry ; Peptides - isolation & purification ; Peptidyl-Dipeptidase A - metabolism ; Properties ; Rats ; Rats, Inbred SHR</subject><ispartof>BioMed research international, 2013-01, Vol.2013 (2013), p.1-6</ispartof><rights>Copyright © 2013 Min-Gu Kang et al.</rights><rights>COPYRIGHT 2013 John Wiley & Sons, Inc.</rights><rights>Copyright © 2013 Min-Gu Kang et al. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c430t-439b6a57ec5f62a97e477111c271a4f401e3d2ea3c1636a02a4db0bd8a4394de3</citedby><cites>FETCH-LOGICAL-c430t-439b6a57ec5f62a97e477111c271a4f401e3d2ea3c1636a02a4db0bd8a4394de3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3860087/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3860087/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24380081$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Choi, Youngjun</contributor><creatorcontrib>Seo, Geon-Sik</creatorcontrib><creatorcontrib>Kim, Min-Kyung</creatorcontrib><creatorcontrib>Bolormaa, Zanabaatar</creatorcontrib><creatorcontrib>Kim, Young-Hun</creatorcontrib><creatorcontrib>Kang, Min-Gu</creatorcontrib><creatorcontrib>Lee, Jong-Soo</creatorcontrib><title>Characterization of an Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Peptide from the Edible Mushroom Hypsizygus marmoreus</title><title>BioMed research international</title><addtitle>Biomed Res Int</addtitle><description>Hypertension is one of the very serious diseases and, recently, hypertensive patient longevity has been increased significantly. Therefore, the development of new antihypertensive drugs or bioactive compounds is very important to remedy or prevent hypertension. The antihypertensive angiotensin I-converting enzyme (ACE) inhibitor in water extracts from the brown-cultivar-fruiting-body of Hypsizygus marmoreus was purified with ultrafiltration, C18 solid phase extraction chromatography and reverse-phase HPLC, and the purified ACE inhibitor with inhibitory activity of IC50 value of 0.19 mg/mL was obtained. The purified ACE inhibitor was found to be a new oligopeptide with the sequence LSMGSASLSP. Its molecular weight was estimated to be 567.3 Da and the water extracts containing ACE inhibitor from Hypsizygus marmoreus showed a clear antihypertensive action a spontaneously hypertensive rat.</description><subject>Agaricales - enzymology</subject><subject>Angiotensin converting enzyme</subject><subject>Angiotensin-Converting Enzyme Inhibitors - administration & dosage</subject><subject>Angiotensin-Converting Enzyme Inhibitors - chemistry</subject><subject>Angiotensin-Converting Enzyme Inhibitors - isolation & purification</subject><subject>Animals</subject><subject>Antihypertensive Agents - administration & dosage</subject><subject>Antihypertensive Agents - chemistry</subject><subject>Basidiomycota</subject><subject>Biological products</subject><subject>Blood Pressure - drug effects</subject><subject>Care and treatment</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Hypertension</subject><subject>Hypertension - drug therapy</subject><subject>Hypertension - pathology</subject><subject>Identification and classification</subject><subject>Peptides - administration & dosage</subject><subject>Peptides - chemistry</subject><subject>Peptides - isolation & purification</subject><subject>Peptidyl-Dipeptidase A - metabolism</subject><subject>Properties</subject><subject>Rats</subject><subject>Rats, Inbred SHR</subject><issn>2314-6133</issn><issn>2314-6141</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><sourceid>EIF</sourceid><recordid>eNqNkU9v1DAQxSMEolXpiTuyxAWBQu3Y-XdBWq0WulIRHOBsTZJJYpTYi-1slf0EfGwcUlblhi_2zPzm6ckvil4y-p6xNL1JKOM3ScHLTDyJLhPORJwxwZ6e35xfRNfO_aDhFCyjZfY8ukgEL5byMvq17cFC7dGqE3hlNDEtAU022qt-PqD1qJ06Ymh0yvwpNNnHW6OPYaZ0R3b6NI9I9rpXlfLGzuQrHrxqkLTWjMT3SHaNqgYknyfXWxN6t_PBqdPcTY6MYEdjcXIvomctDA6vH-6r6PvH3bftbXz35dN-u7mLa8GpjwUvqwzSHOu0zRIocxR5zhirk5yBaAVlyJsEgdcs4xnQBERT0aopIGyKBvlV9GHVPUzViE2N2lsY5MGqYGWWBpT8d6JVLztzlLzIwpflQeDNg4A1Pyd0Xo7K1TgMoNFMTjJR0lxQzhf09Yp2MKBUujVBsV5wuQljniciTQP1bqVqa5yz2J7NMCqXkOUSslxDDvSrx_7P7N9IA_B2BXqlG7hX_6eGAcEWHsGUFyXlvwF4mLsP</recordid><startdate>20130101</startdate><enddate>20130101</enddate><creator>Seo, Geon-Sik</creator><creator>Kim, Min-Kyung</creator><creator>Bolormaa, Zanabaatar</creator><creator>Kim, Young-Hun</creator><creator>Kang, Min-Gu</creator><creator>Lee, Jong-Soo</creator><general>Hindawi Publishing Corporation</general><general>John Wiley & Sons, Inc</general><scope>ADJCN</scope><scope>AHFXO</scope><scope>RHU</scope><scope>RHW</scope><scope>RHX</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20130101</creationdate><title>Characterization of an Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Peptide from the Edible Mushroom Hypsizygus marmoreus</title><author>Seo, Geon-Sik ; 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| subjects | Agaricales - enzymology Angiotensin converting enzyme Angiotensin-Converting Enzyme Inhibitors - administration & dosage Angiotensin-Converting Enzyme Inhibitors - chemistry Angiotensin-Converting Enzyme Inhibitors - isolation & purification Animals Antihypertensive Agents - administration & dosage Antihypertensive Agents - chemistry Basidiomycota Biological products Blood Pressure - drug effects Care and treatment Chromatography, High Pressure Liquid Health aspects Humans Hypertension Hypertension - drug therapy Hypertension - pathology Identification and classification Peptides - administration & dosage Peptides - chemistry Peptides - isolation & purification Peptidyl-Dipeptidase A - metabolism Properties Rats Rats, Inbred SHR |
| title | Characterization of an Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Peptide from the Edible Mushroom Hypsizygus marmoreus |
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