Cation-stimulated adenosine triphosphatase activity and cation transport in corn roots

Cation-stimulated adenosine triphosphatase activity and cation transport in corn roots

ATPase activity of the plasma membrane fraction from primary roots of corn (Zea mays L. WF9 × M14) was activated by Mg2+ and further stimulated by monovalent cations (K+ > Rb+ > Cs+ > Na+ > Li+). K+-stimulated activity required Mg2+ and was substrate-specific. Maximum ATPase activity in...

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Veröffentlicht in:Plant physiology (Bethesda) 1976-09, Vol.58 (3), p.331-335
Hauptverfasser: Leonard, R.T, Hotchkiss, C.W
Format: Artikel
Sprache:eng
Schlagworte:
Adenosine triphosphatases
Calcium
Cell membranes
Corn
Enzymes
Kinetics
Oats
Oligomycins
Plant roots
Plants
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Hotchkiss, C.W
description ATPase activity of the plasma membrane fraction from primary roots of corn (Zea mays L. WF9 × M14) was activated by Mg2+ and further stimulated by monovalent cations (K+ > Rb+ > Cs+ > Na+ > Li+). K+-stimulated activity required Mg2+ and was substrate-specific. Maximum ATPase activity in the presence of Mg2+ and K+ was at pH 6.5 and 40 C. Calcium and lanthanum (
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WF9 × M14) was activated by Mg2+ and further stimulated by monovalent cations (K+ &gt; Rb+ &gt; Cs+ &gt; Na+ &gt; Li+). K+-stimulated activity required Mg2+ and was substrate-specific. Maximum ATPase activity in the presence of Mg2+ and K+ was at pH 6.5 and 40 C. Calcium and lanthanum (&lt;0.5 mM) were inhibitors of ATPase, but only in the presence of Mg2+. Oligomycin was not an inhibitor of the plasma membrane ATPase, whereas N,N′-dicyclohexylcarbodiimide was. Activity showed a simple Michaelis-Menten saturation with increasing ATP·Mg. The major effect of K+ in stimulating ATPase activity was on maximum velocity. The kinetic data of K+ stimulation were complex, but similar to the kinetics of short term K+ influx in corn roots. Both K+-ATPase and K+ influx kinetics met all criteria for negative cooperativity. The results provided further support for the concept that cation transport in plants is energized by ATP, and mediated by a cation-ATPase on the plasma membrane.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.58.3.331</identifier><identifier>PMID: 16659673</identifier><language>eng</language><publisher>United States: American Society of Plant Physiologists</publisher><subject>Adenosine triphosphatases ; Calcium ; Cell membranes ; Corn ; Enzymes ; Kinetics ; Oats ; Oligomycins ; Plant roots ; Plants</subject><ispartof>Plant physiology (Bethesda), 1976-09, Vol.58 (3), p.331-335</ispartof><rights>Copyright 1976 The American Society of Plant Physiologists</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c384t-e6e456d46c6b29423642806445e5c2d3e0b7f9812adaabf338831c86df3375793</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4264550$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4264550$$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/16659673$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leonard, R.T</creatorcontrib><creatorcontrib>Hotchkiss, C.W</creatorcontrib><title>Cation-stimulated adenosine triphosphatase activity and cation transport in corn roots</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>ATPase activity of the plasma membrane fraction from primary roots of corn (Zea mays L. WF9 × M14) was activated by Mg2+ and further stimulated by monovalent cations (K+ &gt; Rb+ &gt; Cs+ &gt; Na+ &gt; Li+). K+-stimulated activity required Mg2+ and was substrate-specific. Maximum ATPase activity in the presence of Mg2+ and K+ was at pH 6.5 and 40 C. Calcium and lanthanum (&lt;0.5 mM) were inhibitors of ATPase, but only in the presence of Mg2+. Oligomycin was not an inhibitor of the plasma membrane ATPase, whereas N,N′-dicyclohexylcarbodiimide was. Activity showed a simple Michaelis-Menten saturation with increasing ATP·Mg. The major effect of K+ in stimulating ATPase activity was on maximum velocity. The kinetic data of K+ stimulation were complex, but similar to the kinetics of short term K+ influx in corn roots. Both K+-ATPase and K+ influx kinetics met all criteria for negative cooperativity. The results provided further support for the concept that cation transport in plants is energized by ATP, and mediated by a cation-ATPase on the plasma membrane.</description><subject>Adenosine triphosphatases</subject><subject>Calcium</subject><subject>Cell membranes</subject><subject>Corn</subject><subject>Enzymes</subject><subject>Kinetics</subject><subject>Oats</subject><subject>Oligomycins</subject><subject>Plant roots</subject><subject>Plants</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><recordid>eNpVkc2LFDEQxYMo7uzqyZuI9G0P0mOSStLpgwcZ_IIFD7peQ006vZOlJ4lJZmH_e6MzrHqqgvd7VY8qQl4wumaMircpraVewxqAPSIrJoH3XAr9mKwobT3Vejwj56XcUkoZMPGUnDGl5KgGWJEfG6w-hr5Uvz8sWN3U4eRCLD64rmafdrGkHVYsrkNb_Z2v9x2GqbN_fA3BUFLMtfOhszGHLsdYyzPyZMaluOenekGuP374vvncX3399GXz_qq3oEXtnXJCqkkoq7Z8FByU4JoqIaSTlk_g6HaYR804TojbGUBrYFarqbWDHEa4IO-Oc9Nhu3eTdaEFWkzKfo_53kT05n8l-J25iXdGCs4Fa_7Lkz_HnwdXqtn7Yt2yYHDxUMwAILSimjfyzZG0OZaS3fywhFHz-w8mJSO1AdP-0OjX_-b6y54O34BXR-C21JgfdMGVkJI2-eVRnjEavMm-mOtvg2JajRx-ATVZlzk</recordid><startdate>19760901</startdate><enddate>19760901</enddate><creator>Leonard, R.T</creator><creator>Hotchkiss, C.W</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>19760901</creationdate><title>Cation-stimulated adenosine triphosphatase activity and cation transport in corn roots</title><author>Leonard, R.T ; Hotchkiss, C.W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c384t-e6e456d46c6b29423642806445e5c2d3e0b7f9812adaabf338831c86df3375793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Adenosine triphosphatases</topic><topic>Calcium</topic><topic>Cell membranes</topic><topic>Corn</topic><topic>Enzymes</topic><topic>Kinetics</topic><topic>Oats</topic><topic>Oligomycins</topic><topic>Plant roots</topic><topic>Plants</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leonard, R.T</creatorcontrib><creatorcontrib>Hotchkiss, C.W</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>Leonard, R.T</au><au>Hotchkiss, C.W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cation-stimulated adenosine triphosphatase activity and cation transport in corn roots</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1976-09-01</date><risdate>1976</risdate><volume>58</volume><issue>3</issue><spage>331</spage><epage>335</epage><pages>331-335</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><abstract>ATPase activity of the plasma membrane fraction from primary roots of corn (Zea mays L. WF9 × M14) was activated by Mg2+ and further stimulated by monovalent cations (K+ &gt; Rb+ &gt; Cs+ &gt; Na+ &gt; Li+). K+-stimulated activity required Mg2+ and was substrate-specific. Maximum ATPase activity in the presence of Mg2+ and K+ was at pH 6.5 and 40 C. Calcium and lanthanum (&lt;0.5 mM) were inhibitors of ATPase, but only in the presence of Mg2+. Oligomycin was not an inhibitor of the plasma membrane ATPase, whereas N,N′-dicyclohexylcarbodiimide was. Activity showed a simple Michaelis-Menten saturation with increasing ATP·Mg. The major effect of K+ in stimulating ATPase activity was on maximum velocity. The kinetic data of K+ stimulation were complex, but similar to the kinetics of short term K+ influx in corn roots. Both K+-ATPase and K+ influx kinetics met all criteria for negative cooperativity. The results provided further support for the concept that cation transport in plants is energized by ATP, and mediated by a cation-ATPase on the plasma membrane.</abstract><cop>United States</cop><pub>American Society of Plant Physiologists</pub><pmid>16659673</pmid><doi>10.1104/pp.58.3.331</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
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source Jstor Complete Legacy; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection
subjects Adenosine triphosphatases
Calcium
Cell membranes
Corn
Enzymes
Kinetics
Oats
Oligomycins
Plant roots
Plants
title Cation-stimulated adenosine triphosphatase activity and cation transport in corn roots
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