Multiple amine oxidases in cucumber seedlings
Cell-free extracts of cucumber (Cucumis sativus L. cv. National Pickling) seedlings were found to have amine oxidase activity when assayed with tryptamine as a substrate. Studies of the effect of lowered pH on the extract indicated that this activity was heterogeneous, and three amine oxidases could...
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| Veröffentlicht in: | Plant physiology (Bethesda) 1974-10, Vol.54 (4), p.601-607 |
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| container_title | Plant physiology (Bethesda) |
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| creator | Frank W. Percival Purves, William K. |
| description | Cell-free extracts of cucumber (Cucumis sativus L. cv. National Pickling) seedlings were found to have amine oxidase activity when assayed with tryptamine as a substrate. Studies of the effect of lowered pH on the extract indicated that this activity was heterogeneous, and three amine oxidases could be separated by ion exchange chromatography. The partially purified enzymes were tested for their activities with several substrates and for their sensitivities to various amine oxidase inhibitors. One of the enzymes may be a monoamine oxidase, although it is inhibited by some diamine oxidase inhibitors. The other two enzymes have properties more characteristic of the diamine oxidases. The possible relationship of the amine oxidases to indoleacetic acid biosynthesis in cucumber seedlings is discussed. |
| doi_str_mv | 10.1104/pp.54.4.601 |
| format | Article |
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Percival ; Purves, William K.</creator><creatorcontrib>Frank W. Percival ; Purves, William K. ; Hohenheim Univ. (Germany, F.R.). Fachbereich Biologie und Allgemeine Naturwissenschaften</creatorcontrib><description>Cell-free extracts of cucumber (Cucumis sativus L. cv. National Pickling) seedlings were found to have amine oxidase activity when assayed with tryptamine as a substrate. Studies of the effect of lowered pH on the extract indicated that this activity was heterogeneous, and three amine oxidases could be separated by ion exchange chromatography. The partially purified enzymes were tested for their activities with several substrates and for their sensitivities to various amine oxidase inhibitors. One of the enzymes may be a monoamine oxidase, although it is inhibited by some diamine oxidase inhibitors. The other two enzymes have properties more characteristic of the diamine oxidases. The possible relationship of the amine oxidases to indoleacetic acid biosynthesis in cucumber seedlings is discussed.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.54.4.601</identifier><identifier>PMID: 16658936</identifier><language>eng</language><publisher>United States: American Society of Plant Physiologists</publisher><subject>Amines ; Cucumbers ; Diamines ; Enzymes ; Oxidases ; Peas ; Phosphates ; Seedlings ; Sodium ; Substrate specificity</subject><ispartof>Plant physiology (Bethesda), 1974-10, Vol.54 (4), p.601-607</ispartof><rights>Copyright 1974 The American Society of Plant Physiologists</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-65e1496646f252d283bc744056c9cb31dc47b51d95e2d172732306cb5d41b6503</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4263777$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4263777$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16658936$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Frank W. Percival</creatorcontrib><creatorcontrib>Purves, William K.</creatorcontrib><creatorcontrib>Hohenheim Univ. (Germany, F.R.). Fachbereich Biologie und Allgemeine Naturwissenschaften</creatorcontrib><title>Multiple amine oxidases in cucumber seedlings</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>Cell-free extracts of cucumber (Cucumis sativus L. cv. National Pickling) seedlings were found to have amine oxidase activity when assayed with tryptamine as a substrate. Studies of the effect of lowered pH on the extract indicated that this activity was heterogeneous, and three amine oxidases could be separated by ion exchange chromatography. The partially purified enzymes were tested for their activities with several substrates and for their sensitivities to various amine oxidase inhibitors. One of the enzymes may be a monoamine oxidase, although it is inhibited by some diamine oxidase inhibitors. The other two enzymes have properties more characteristic of the diamine oxidases. The possible relationship of the amine oxidases to indoleacetic acid biosynthesis in cucumber seedlings is discussed.</description><subject>Amines</subject><subject>Cucumbers</subject><subject>Diamines</subject><subject>Enzymes</subject><subject>Oxidases</subject><subject>Peas</subject><subject>Phosphates</subject><subject>Seedlings</subject><subject>Sodium</subject><subject>Substrate specificity</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><recordid>eNpVkTlPAzEQhS0EIuGoaBHajgJt8DE-tqBAEZcURAGpLa_XCY72wt5F8O9ZlCiBakZ635sZvUHojOAJIRiu23bCYQITgckeGhPOaEo5qH00xnjosVLZCB3FuMIYE0bgEI2IEFxlTIxR-tyXnW9Ll5jK1y5pvnxhoouJrxPb277KXUiic0Xp62U8QQcLU0Z3uqnHaH5_9zZ9TGcvD0_T21lqmVJdKrgjkAkBYkE5LahiuZUAmAub2ZyRwoLMOSky7mhBJJWMMixszgsgueCYHaOb9dy2zytXWFd3wZS6Db4y4Vs3xuv_Su3f9bL51ExIEGTwX278ofnoXex05aN1ZWlq1_RRS8ZAgcRqIK_WpA1NjMEttksI1r_x6rbVHDToId6Bvvh7147d5DkA52tgFbsmbHWggkkpd_6FabRZBh_1_JVkkg-vEVIq9gN4wYdm</recordid><startdate>19741001</startdate><enddate>19741001</enddate><creator>Frank W. Percival</creator><creator>Purves, William K.</creator><general>American Society of Plant Physiologists</general><scope>FBQ</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19741001</creationdate><title>Multiple amine oxidases in cucumber seedlings</title><author>Frank W. Percival ; Purves, William K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-65e1496646f252d283bc744056c9cb31dc47b51d95e2d172732306cb5d41b6503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1974</creationdate><topic>Amines</topic><topic>Cucumbers</topic><topic>Diamines</topic><topic>Enzymes</topic><topic>Oxidases</topic><topic>Peas</topic><topic>Phosphates</topic><topic>Seedlings</topic><topic>Sodium</topic><topic>Substrate specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Frank W. Percival</creatorcontrib><creatorcontrib>Purves, William K.</creatorcontrib><creatorcontrib>Hohenheim Univ. (Germany, F.R.). Fachbereich Biologie und Allgemeine Naturwissenschaften</creatorcontrib><collection>AGRIS</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Frank W. Percival</au><au>Purves, William K.</au><aucorp>Hohenheim Univ. (Germany, F.R.). Fachbereich Biologie und Allgemeine Naturwissenschaften</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Multiple amine oxidases in cucumber seedlings</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1974-10-01</date><risdate>1974</risdate><volume>54</volume><issue>4</issue><spage>601</spage><epage>607</epage><pages>601-607</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><abstract>Cell-free extracts of cucumber (Cucumis sativus L. cv. National Pickling) seedlings were found to have amine oxidase activity when assayed with tryptamine as a substrate. Studies of the effect of lowered pH on the extract indicated that this activity was heterogeneous, and three amine oxidases could be separated by ion exchange chromatography. The partially purified enzymes were tested for their activities with several substrates and for their sensitivities to various amine oxidase inhibitors. One of the enzymes may be a monoamine oxidase, although it is inhibited by some diamine oxidase inhibitors. The other two enzymes have properties more characteristic of the diamine oxidases. The possible relationship of the amine oxidases to indoleacetic acid biosynthesis in cucumber seedlings is discussed.</abstract><cop>United States</cop><pub>American Society of Plant Physiologists</pub><pmid>16658936</pmid><doi>10.1104/pp.54.4.601</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Plant physiology (Bethesda), 1974-10, Vol.54 (4), p.601-607 |
| issn | 0032-0889 1532-2548 |
| language | eng |
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| source | Jstor Complete Legacy; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Amines Cucumbers Diamines Enzymes Oxidases Peas Phosphates Seedlings Sodium Substrate specificity |
| title | Multiple amine oxidases in cucumber seedlings |
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