Transport of phenylalanine into vacuoles isolated from barley mesophyll protoplasts
The energy-dependent transport of phenylalanine into isolated vacuoles of barley (Hordeum vulgare L.) mesophyll protoplasts has been studied by silicone-layer floatation filtering. The uptake of this aromatic amino acid into the vacuolar compartment is markedly increased by MgATP, showing saturation...
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Veröffentlicht in: | Planta 1988-12, Vol.176 (3), p.378-382 |
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description | The energy-dependent transport of phenylalanine into isolated vacuoles of barley (Hordeum vulgare L.) mesophyll protoplasts has been studied by silicone-layer floatation filtering. The uptake of this aromatic amino acid into the vacuolar compartment is markedly increased by MgATP, showing saturation kinetics; the Km values were 0.5 mM for MgATP and 1.2 mM for phenylalanine. Vmax for phenylalanine transport was estimated to 140 nmol phenylalanine·(mg·Chl)-1·h-1. The transport shows a distinct pH optimum at 7.3 and is markedly inhibited by 40 mM nitrate. Azide (1 mM) and vanadate (400 μM) had no or little effect on rates of transport while p-fluorophenylalanine seemed to be an effective inhibitor, indicating a possible competition at an amino-acid carrier. Ionophores such as valinomycin, nigericin or gramicidin were strong inhibitors of phenylalanine transport, indicating that this process is coupled to both the transmembrane pH gradient (ΔpH) and the transmembrane potential (Δψ). |
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(Tieraerztliche Hochschule Hannover (Germany, F.R.)) ; Schultz, G</creator><creatorcontrib>Homeyer, U. (Tieraerztliche Hochschule Hannover (Germany, F.R.)) ; Schultz, G</creatorcontrib><description>The energy-dependent transport of phenylalanine into isolated vacuoles of barley (Hordeum vulgare L.) mesophyll protoplasts has been studied by silicone-layer floatation filtering. The uptake of this aromatic amino acid into the vacuolar compartment is markedly increased by MgATP, showing saturation kinetics; the Km values were 0.5 mM for MgATP and 1.2 mM for phenylalanine. Vmax for phenylalanine transport was estimated to 140 nmol phenylalanine·(mg·Chl)-1·h-1. The transport shows a distinct pH optimum at 7.3 and is markedly inhibited by 40 mM nitrate. Azide (1 mM) and vanadate (400 μM) had no or little effect on rates of transport while p-fluorophenylalanine seemed to be an effective inhibitor, indicating a possible competition at an amino-acid carrier. Ionophores such as valinomycin, nigericin or gramicidin were strong inhibitors of phenylalanine transport, indicating that this process is coupled to both the transmembrane pH gradient (ΔpH) and the transmembrane potential (Δψ).</description><identifier>ISSN: 0032-0935</identifier><identifier>EISSN: 1432-2048</identifier><identifier>DOI: 10.1007/BF00395418</identifier><identifier>PMID: 24220866</identifier><identifier>CODEN: PLANAB</identifier><language>eng</language><publisher>Berlin: Springer-Verlag</publisher><subject>ABSORCION ; ABSORPTION ; Amino acids ; Aminosaeuretransport ; Aufnahme ; Azides ; Barley ; Biological and medical sciences ; Blattgewebe ; Cell physiology ; Chloroplasts ; Enzymes ; FENILALANINA ; Fundamental and applied biological sciences. Psychology ; Hordeum ; HORDEUM VULGARE ; Mesophyll ; Nitrates ; PHENYLALANINE ; Plant physiology and development ; Plants ; Plasma membrane and permeation ; PROTOPLASM ; PROTOPLASMA ; PROTOPLASME ; Protoplast ; Protoplasts ; TRANSLOCACION ; TRANSLOCATION ; VACUOLA ; VACUOLE ; VACUOLES ; Vakuole</subject><ispartof>Planta, 1988-12, Vol.176 (3), p.378-382</ispartof><rights>Springer-Verlag Berlin Heidelberg 1988</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c355t-551955e064f24cddc585c3605e5c22d48bee6948391579631e1a6909a43d7b03</citedby><cites>FETCH-LOGICAL-c355t-551955e064f24cddc585c3605e5c22d48bee6948391579631e1a6909a43d7b03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/23379461$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/23379461$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6635974$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24220866$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Homeyer, U. (Tieraerztliche Hochschule Hannover (Germany, F.R.))</creatorcontrib><creatorcontrib>Schultz, G</creatorcontrib><title>Transport of phenylalanine into vacuoles isolated from barley mesophyll protoplasts</title><title>Planta</title><addtitle>Planta</addtitle><description>The energy-dependent transport of phenylalanine into isolated vacuoles of barley (Hordeum vulgare L.) mesophyll protoplasts has been studied by silicone-layer floatation filtering. The uptake of this aromatic amino acid into the vacuolar compartment is markedly increased by MgATP, showing saturation kinetics; the Km values were 0.5 mM for MgATP and 1.2 mM for phenylalanine. Vmax for phenylalanine transport was estimated to 140 nmol phenylalanine·(mg·Chl)-1·h-1. The transport shows a distinct pH optimum at 7.3 and is markedly inhibited by 40 mM nitrate. Azide (1 mM) and vanadate (400 μM) had no or little effect on rates of transport while p-fluorophenylalanine seemed to be an effective inhibitor, indicating a possible competition at an amino-acid carrier. Ionophores such as valinomycin, nigericin or gramicidin were strong inhibitors of phenylalanine transport, indicating that this process is coupled to both the transmembrane pH gradient (ΔpH) and the transmembrane potential (Δψ).</description><subject>ABSORCION</subject><subject>ABSORPTION</subject><subject>Amino acids</subject><subject>Aminosaeuretransport</subject><subject>Aufnahme</subject><subject>Azides</subject><subject>Barley</subject><subject>Biological and medical sciences</subject><subject>Blattgewebe</subject><subject>Cell physiology</subject><subject>Chloroplasts</subject><subject>Enzymes</subject><subject>FENILALANINA</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hordeum</subject><subject>HORDEUM VULGARE</subject><subject>Mesophyll</subject><subject>Nitrates</subject><subject>PHENYLALANINE</subject><subject>Plant physiology and development</subject><subject>Plants</subject><subject>Plasma membrane and permeation</subject><subject>PROTOPLASM</subject><subject>PROTOPLASMA</subject><subject>PROTOPLASME</subject><subject>Protoplast</subject><subject>Protoplasts</subject><subject>TRANSLOCACION</subject><subject>TRANSLOCATION</subject><subject>VACUOLA</subject><subject>VACUOLE</subject><subject>VACUOLES</subject><subject>Vakuole</subject><issn>0032-0935</issn><issn>1432-2048</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><recordid>eNpF0MtL7DAYBfAgV3R8bFxe8JKFCxGqebbJ0reC4MLZl0z69VpJm5qvI8x_b2RGXQVyfpyEQ8gRZ-ecseri6o4xabXiZovMuJKiEEyZP2SWr0XBrNS7ZA_xjbEcVtUO2RVKCGbKckZe5skNOMY00djS8RWGVXDBDd0AtBumSD-cX8YASDuMwU3Q0DbFni5cCrCiPWAcX1ch0DHFKY7B4YQHZLt1AeFwc-6T-d3t_PqheHq-f7y-fCq81HoqtOZWa2ClaoXyTeO10V6WTIP2QjTKLABKq4y0XFe2lBy4Ky2zTsmmWjC5T07Xtfnp9yXgVPcdegj59xCXWHOVC5kw2mR6tqY-RcQEbT2mrndpVXNWf21Y_26Y8b9N73LRQ_NDv0fL4GQDHHoX2ryg7_DHZaFtpTI7XrM3nGL6rZGysqrkOf-7zlsXa_c_5YqbW2PuuZCV_AQJK4n0</recordid><startdate>19881201</startdate><enddate>19881201</enddate><creator>Homeyer, U. 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(Tieraerztliche Hochschule Hannover (Germany, F.R.)) ; Schultz, G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c355t-551955e064f24cddc585c3605e5c22d48bee6948391579631e1a6909a43d7b03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>ABSORCION</topic><topic>ABSORPTION</topic><topic>Amino acids</topic><topic>Aminosaeuretransport</topic><topic>Aufnahme</topic><topic>Azides</topic><topic>Barley</topic><topic>Biological and medical sciences</topic><topic>Blattgewebe</topic><topic>Cell physiology</topic><topic>Chloroplasts</topic><topic>Enzymes</topic><topic>FENILALANINA</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hordeum</topic><topic>HORDEUM VULGARE</topic><topic>Mesophyll</topic><topic>Nitrates</topic><topic>PHENYLALANINE</topic><topic>Plant physiology and development</topic><topic>Plants</topic><topic>Plasma membrane and permeation</topic><topic>PROTOPLASM</topic><topic>PROTOPLASMA</topic><topic>PROTOPLASME</topic><topic>Protoplast</topic><topic>Protoplasts</topic><topic>TRANSLOCACION</topic><topic>TRANSLOCATION</topic><topic>VACUOLA</topic><topic>VACUOLE</topic><topic>VACUOLES</topic><topic>Vakuole</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Homeyer, U. (Tieraerztliche Hochschule Hannover (Germany, F.R.))</creatorcontrib><creatorcontrib>Schultz, G</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Planta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Homeyer, U. (Tieraerztliche Hochschule Hannover (Germany, F.R.))</au><au>Schultz, G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transport of phenylalanine into vacuoles isolated from barley mesophyll protoplasts</atitle><jtitle>Planta</jtitle><addtitle>Planta</addtitle><date>1988-12-01</date><risdate>1988</risdate><volume>176</volume><issue>3</issue><spage>378</spage><epage>382</epage><pages>378-382</pages><issn>0032-0935</issn><eissn>1432-2048</eissn><coden>PLANAB</coden><abstract>The energy-dependent transport of phenylalanine into isolated vacuoles of barley (Hordeum vulgare L.) mesophyll protoplasts has been studied by silicone-layer floatation filtering. The uptake of this aromatic amino acid into the vacuolar compartment is markedly increased by MgATP, showing saturation kinetics; the Km values were 0.5 mM for MgATP and 1.2 mM for phenylalanine. Vmax for phenylalanine transport was estimated to 140 nmol phenylalanine·(mg·Chl)-1·h-1. The transport shows a distinct pH optimum at 7.3 and is markedly inhibited by 40 mM nitrate. Azide (1 mM) and vanadate (400 μM) had no or little effect on rates of transport while p-fluorophenylalanine seemed to be an effective inhibitor, indicating a possible competition at an amino-acid carrier. Ionophores such as valinomycin, nigericin or gramicidin were strong inhibitors of phenylalanine transport, indicating that this process is coupled to both the transmembrane pH gradient (ΔpH) and the transmembrane potential (Δψ).</abstract><cop>Berlin</cop><pub>Springer-Verlag</pub><pmid>24220866</pmid><doi>10.1007/BF00395418</doi><tpages>5</tpages></addata></record> |
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subjects | ABSORCION ABSORPTION Amino acids Aminosaeuretransport Aufnahme Azides Barley Biological and medical sciences Blattgewebe Cell physiology Chloroplasts Enzymes FENILALANINA Fundamental and applied biological sciences. Psychology Hordeum HORDEUM VULGARE Mesophyll Nitrates PHENYLALANINE Plant physiology and development Plants Plasma membrane and permeation PROTOPLASM PROTOPLASMA PROTOPLASME Protoplast Protoplasts TRANSLOCACION TRANSLOCATION VACUOLA VACUOLE VACUOLES Vakuole |
title | Transport of phenylalanine into vacuoles isolated from barley mesophyll protoplasts |
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