Monoamine oxidase activity in hepatopancreas of Octopus vulgaris
1. Monoamine oxidase activity has been studied in hepatopancreas of Octopus vulgaris using 5-HT and PEA as substrates. 2. Time courses of MAO activity against 5-HT and PEA show that the enzyme has higher affinity for PEA than for 5-HT. 3. MAO activity against 5-HT appears more sensitive than MAO act...
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| Veröffentlicht in: | Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology Comparative pharmacology and toxicology, 1993, Vol.106 (2), p.479-482 |
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| container_end_page | 482 |
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| container_issue | 2 |
| container_start_page | 479 |
| container_title | Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology |
| container_volume | 106 |
| creator | Nicotra, Antonietta Senatori, Ornella Santangelo, Giovanni |
| description | 1. Monoamine oxidase activity has been studied in hepatopancreas of
Octopus vulgaris using 5-HT and PEA as substrates.
2. Time courses of MAO activity against 5-HT and PEA show that the enzyme has higher affinity for PEA than for 5-HT.
3. MAO activity against 5-HT appears more sensitive than MAO activity against PEA, to variations of the temperature (range 17–67°C).
4. The inhibition curves obtained with clorgyline and deprenyl indicate that MAO activity is due to a single form of the enzyme, not corresponding to type A and type B MAO.
5. Semicarbazide 10
−4 M does not affect the deamination of 5-HT and PEA, demonstrating that a semicarbazide-sensitive amine oxidase is not involved in this process. |
| doi_str_mv | 10.1016/0742-8413(93)90166-I |
| format | Article |
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Octopus vulgaris using 5-HT and PEA as substrates.
2. Time courses of MAO activity against 5-HT and PEA show that the enzyme has higher affinity for PEA than for 5-HT.
3. MAO activity against 5-HT appears more sensitive than MAO activity against PEA, to variations of the temperature (range 17–67°C).
4. The inhibition curves obtained with clorgyline and deprenyl indicate that MAO activity is due to a single form of the enzyme, not corresponding to type A and type B MAO.
5. Semicarbazide 10
−4 M does not affect the deamination of 5-HT and PEA, demonstrating that a semicarbazide-sensitive amine oxidase is not involved in this process.</description><identifier>ISSN: 0742-8413</identifier><identifier>DOI: 10.1016/0742-8413(93)90166-I</identifier><language>eng</language><publisher>Oxford: Elsevier Inc</publisher><subject>Biochemistry. Physiology. Immunology ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Invertebrates ; Marine ; Mollusca ; Octopus vulgaris ; Physiology. Development</subject><ispartof>Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology, 1993, Vol.106 (2), p.479-482</ispartof><rights>1993</rights><rights>1994 INIST-CNRS</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c364t-ee843dc3753672cfd98570dae903ba6be76e67cd4af31cd7176bfec71ea483743</citedby><cites>FETCH-LOGICAL-c364t-ee843dc3753672cfd98570dae903ba6be76e67cd4af31cd7176bfec71ea483743</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3905996$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Nicotra, Antonietta</creatorcontrib><creatorcontrib>Senatori, Ornella</creatorcontrib><creatorcontrib>Santangelo, Giovanni</creatorcontrib><title>Monoamine oxidase activity in hepatopancreas of Octopus vulgaris</title><title>Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology</title><description>1. Monoamine oxidase activity has been studied in hepatopancreas of
Octopus vulgaris using 5-HT and PEA as substrates.
2. Time courses of MAO activity against 5-HT and PEA show that the enzyme has higher affinity for PEA than for 5-HT.
3. MAO activity against 5-HT appears more sensitive than MAO activity against PEA, to variations of the temperature (range 17–67°C).
4. The inhibition curves obtained with clorgyline and deprenyl indicate that MAO activity is due to a single form of the enzyme, not corresponding to type A and type B MAO.
5. Semicarbazide 10
−4 M does not affect the deamination of 5-HT and PEA, demonstrating that a semicarbazide-sensitive amine oxidase is not involved in this process.</description><subject>Biochemistry. Physiology. Immunology</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Invertebrates</subject><subject>Marine</subject><subject>Mollusca</subject><subject>Octopus vulgaris</subject><subject>Physiology. Development</subject><issn>0742-8413</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><recordid>eNp9UE1LAzEU3IOCtfoPPOxBRA-rSZMmm4soxY9CpRc9h9fkrUa2mzXZLfbfm6WlR-HB4w0z85jJsgtKbimh4o5IPilKTtm1YjcqIaKYH2WjA3ySncb4TQihEypG2cObbzysXYO5_3UWIuZgOrdx3TZ3Tf6FLXS-hcYEhJj7Kl-adPcx3_T1JwQXz7LjCuqI5_s9zj6en95nr8Vi-TKfPS4KwwTvCsSSM2uYnDIhJ6ayqpxKYgEVYSsQK5QChTSWQ8WosZJKsarQSIrASyY5G2dXO982-J8eY6fXLhqsa2jQ91FTIUshGU1EviOa4GMMWOk2uDWEraZEDxXpoQs9dKFVmqEiPU-yy70_RAN1FVJmFw9apshUKZFo9zsapqwbh0FH47AxaF1A02nr3f9__gASF302</recordid><startdate>1993</startdate><enddate>1993</enddate><creator>Nicotra, Antonietta</creator><creator>Senatori, Ornella</creator><creator>Santangelo, Giovanni</creator><general>Elsevier Inc</general><general>Pergamon</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TN</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope></search><sort><creationdate>1993</creationdate><title>Monoamine oxidase activity in hepatopancreas of Octopus vulgaris</title><author>Nicotra, Antonietta ; Senatori, Ornella ; Santangelo, Giovanni</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c364t-ee843dc3753672cfd98570dae903ba6be76e67cd4af31cd7176bfec71ea483743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Biochemistry. Physiology. Immunology</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Invertebrates</topic><topic>Marine</topic><topic>Mollusca</topic><topic>Octopus vulgaris</topic><topic>Physiology. Development</topic><toplevel>online_resources</toplevel><creatorcontrib>Nicotra, Antonietta</creatorcontrib><creatorcontrib>Senatori, Ornella</creatorcontrib><creatorcontrib>Santangelo, Giovanni</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Oceanic Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nicotra, Antonietta</au><au>Senatori, Ornella</au><au>Santangelo, Giovanni</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monoamine oxidase activity in hepatopancreas of Octopus vulgaris</atitle><jtitle>Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology</jtitle><date>1993</date><risdate>1993</risdate><volume>106</volume><issue>2</issue><spage>479</spage><epage>482</epage><pages>479-482</pages><issn>0742-8413</issn><abstract>1. Monoamine oxidase activity has been studied in hepatopancreas of
Octopus vulgaris using 5-HT and PEA as substrates.
2. Time courses of MAO activity against 5-HT and PEA show that the enzyme has higher affinity for PEA than for 5-HT.
3. MAO activity against 5-HT appears more sensitive than MAO activity against PEA, to variations of the temperature (range 17–67°C).
4. The inhibition curves obtained with clorgyline and deprenyl indicate that MAO activity is due to a single form of the enzyme, not corresponding to type A and type B MAO.
5. Semicarbazide 10
−4 M does not affect the deamination of 5-HT and PEA, demonstrating that a semicarbazide-sensitive amine oxidase is not involved in this process.</abstract><cop>Oxford</cop><pub>Elsevier Inc</pub><doi>10.1016/0742-8413(93)90166-I</doi><tpages>4</tpages></addata></record> |
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| ispartof | Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology, 1993, Vol.106 (2), p.479-482 |
| issn | 0742-8413 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16786731 |
| source | Alma/SFX Local Collection |
| subjects | Biochemistry. Physiology. Immunology Biological and medical sciences Fundamental and applied biological sciences. Psychology Invertebrates Marine Mollusca Octopus vulgaris Physiology. Development |
| title | Monoamine oxidase activity in hepatopancreas of Octopus vulgaris |
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