Isolation of angiotensin-converting enzyme inhibitor from tuna muscle
A novel inhibitor of angiotensin-converting enzyme (ACE) has been discovered and isolated in a pure form from acid extract of tuna muscle by successive column chromatographies and HPLC. The final preparation showed IC 50 values of 1 μM and 2 μM for ACEs from bovine and rabbit lungs, respectively. Th...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1988-08, Vol.155 (1), p.332-337 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Kohama, Yasuhiro Matsumoto, Shigeru Oka, Hiroaki Teramoto, Tetsuyuki Okabe, Masaru Mimura, Tsutomu |
| description | A novel inhibitor of angiotensin-converting enzyme (ACE) has been discovered and isolated in a pure form from acid extract of tuna muscle by successive column chromatographies and HPLC. The final preparation showed IC
50 values of 1 μM and 2 μM for ACEs from bovine and rabbit lungs, respectively. The amino acid sequence of the inhibitor has been established as Pro-Thr-His-Ile-Lys-Trp-Gly-Asp by the Edman procedure and carboxypeptidase digestion. |
| doi_str_mv | 10.1016/S0006-291X(88)81089-1 |
| format | Article |
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Psychology</subject><subject>Hydrolases</subject><subject>inhibitors</subject><subject>Marine</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>muscles</subject><subject>Muscles - analysis</subject><subject>Neothunnus macropterus</subject><subject>Oligopeptides - isolation & purification</subject><subject>Rabbits</subject><subject>Tuna</subject><subject>ultrastructure</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMoWqs_obAHET2sJrv5PIkUPwoFDyp4C9nsbI3sJprsFvTX29rSq6dhmGfeGR6EJgRfEUz49TPGmOeFIm8XUl5KgqXKyR4aEaxwXhBM99Fohxyh45Q-MCaEcnWIDktKGJdyhO5mKbSmd8FnocmMX7jQg0_O5zb4JcTe-UUG_ue7g8z5d1e5PsSsiaHL-sGbrBuSbeEEHTSmTXC6rWP0en_3Mn3M508Ps-ntPLdU8j4XVaUqSgvFmDANkw21UFhaQA0NLSsmK2NLqpQt-Kq3vDQ1w6xWXAATvOblGJ1vcj9j-Bog9bpzyULbGg9hSFpIikUpin9BwgiTCq8T2Qa0MaQUodGf0XUmfmuC9dqz_vOs1xK1lPrPsyarvcn2wFB1UO-2tmJX87Pt3CRr2iYab13aYVxwocp1zM0Gg5W1pYOok3XgLdQugu11Hdw_j_wCGruahw</recordid><startdate>19880830</startdate><enddate>19880830</enddate><creator>Kohama, Yasuhiro</creator><creator>Matsumoto, Shigeru</creator><creator>Oka, Hiroaki</creator><creator>Teramoto, Tetsuyuki</creator><creator>Okabe, Masaru</creator><creator>Mimura, Tsutomu</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19880830</creationdate><title>Isolation of angiotensin-converting enzyme inhibitor from tuna muscle</title><author>Kohama, Yasuhiro ; Matsumoto, Shigeru ; Oka, Hiroaki ; Teramoto, Tetsuyuki ; Okabe, Masaru ; Mimura, Tsutomu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c486t-7bb9b4429557af58f4ce2c42edef43b58bac3499c26f43c63ad505d967e576d63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Angiotensin-Converting Enzyme Inhibitors - isolation & purification</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>chromatographic techniques</topic><topic>Chromatography, Gel</topic><topic>Chromatography, High Pressure Liquid</topic><topic>dipeptidyl carboxypeptidase I</topic><topic>enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. 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The final preparation showed IC
50 values of 1 μM and 2 μM for ACEs from bovine and rabbit lungs, respectively. The amino acid sequence of the inhibitor has been established as Pro-Thr-His-Ile-Lys-Trp-Gly-Asp by the Edman procedure and carboxypeptidase digestion.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3415688</pmid><doi>10.1016/S0006-291X(88)81089-1</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1988-08, Vol.155 (1), p.332-337 |
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| language | eng |
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| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Angiotensin-Converting Enzyme Inhibitors - isolation & purification Animals Biological and medical sciences Cattle chromatographic techniques Chromatography, Gel Chromatography, High Pressure Liquid dipeptidyl carboxypeptidase I enzymes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases inhibitors Marine Molecular Sequence Data Molecular Weight muscles Muscles - analysis Neothunnus macropterus Oligopeptides - isolation & purification Rabbits Tuna ultrastructure |
| title | Isolation of angiotensin-converting enzyme inhibitor from tuna muscle |
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