protochlorophyllide holochrome of barley (Hordeum vulgare L.). Isolation and characterization of the NADPH: protochlorophyllide oxidoreductase
The NADPH:protochlorophyllide oxidoreductase of barley has been solubilized from etioplast membranes and purified to apparent homogeneity. The highest specific activity measured for the purified enzyme was 1.6 nmol chlorophyllide formed (mg protein-1) per flash. Electrophoretic analysis of the purif...
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| Veröffentlicht in: | European journal of biochemistry 1980-10, Vol.111 (1), p.251-258 |
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| creator | Apel, K Santel, H.J Redlinger, T.E Falk, H |
| description | The NADPH:protochlorophyllide oxidoreductase of barley has been solubilized from etioplast membranes and purified to apparent homogeneity. The highest specific activity measured for the purified enzyme was 1.6 nmol chlorophyllide formed (mg protein-1) per flash. Electrophoretic analysis of the purified enzyme on sodium dodecylsulfate/polyacrylamide gels revealed only one polypeptide of Mr 36000. Durig glycerol gradient centrifugation the enzyme migrates as a low-molecular-weight component. It is proposed that each enzyme molecule contains only one polypeptide chain. Assuming a molecular weight of 36000 for the enzyme, it was calculated that two or three protochlorophyllide molecules are bound to each enzyme molecule. |
| doi_str_mv | 10.1111/j.1432-1033.1980.tb06100.x |
| format | Article |
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Assuming a molecular weight of 36000 for the enzyme, it was calculated that two or three protochlorophyllide molecules are bound to each enzyme molecule.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1980.tb06100.x</identifier><identifier>PMID: 7439188</identifier><language>eng</language><publisher>England</publisher><subject>Chlorophyll - analogs & derivatives ; Hordeum - enzymology ; Kinetics ; Microscopy, Electron ; Molecular Weight ; Oxidoreductases - isolation & purification ; Oxidoreductases - metabolism ; Oxidoreductases Acting on CH-CH Group Donors ; plant biochemistry ; plant physiology ; Plants - enzymology ; Protochlorophyllide - metabolism</subject><ispartof>European journal of biochemistry, 1980-10, Vol.111 (1), p.251-258</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c281t-c9ce675862877dbd15b98172f416dc37f0541902851910c34ed82245dee9b37c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27928,27929</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7439188$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Apel, K</creatorcontrib><creatorcontrib>Santel, H.J</creatorcontrib><creatorcontrib>Redlinger, T.E</creatorcontrib><creatorcontrib>Falk, H</creatorcontrib><title>protochlorophyllide holochrome of barley (Hordeum vulgare L.). Isolation and characterization of the NADPH: protochlorophyllide oxidoreductase</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The NADPH:protochlorophyllide oxidoreductase of barley has been solubilized from etioplast membranes and purified to apparent homogeneity. The highest specific activity measured for the purified enzyme was 1.6 nmol chlorophyllide formed (mg protein-1) per flash. Electrophoretic analysis of the purified enzyme on sodium dodecylsulfate/polyacrylamide gels revealed only one polypeptide of Mr 36000. Durig glycerol gradient centrifugation the enzyme migrates as a low-molecular-weight component. It is proposed that each enzyme molecule contains only one polypeptide chain. Assuming a molecular weight of 36000 for the enzyme, it was calculated that two or three protochlorophyllide molecules are bound to each enzyme molecule.</description><subject>Chlorophyll - analogs & derivatives</subject><subject>Hordeum - enzymology</subject><subject>Kinetics</subject><subject>Microscopy, Electron</subject><subject>Molecular Weight</subject><subject>Oxidoreductases - isolation & purification</subject><subject>Oxidoreductases - metabolism</subject><subject>Oxidoreductases Acting on CH-CH Group Donors</subject><subject>plant biochemistry</subject><subject>plant physiology</subject><subject>Plants - enzymology</subject><subject>Protochlorophyllide - metabolism</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptUU1v1DAQtRBVWQo_AWFxQHBI8Ecc271VBbqVVgUJerYce9Jk5ay3doJ2-RH9zWS1q54YjTTSvHkzo_cQ-kBJSef4si5pxVlBCecl1YqUY0NqSki5e4EWz9BLtCCEVgXTon6FXue8JoTUupbn6FxWXFOlFuhpm-IYXRdiittuH0LvAXcxzK0UB8CxxY1NAfb40zImD9OA_0zhwSbAq_JziW9zDHbs4wbbjceus8m6EVL_99ic6WMH-O7q68_lJf7frbjrfUzgJzfaDG_QWWtDhreneoHuv3_7fb0sVj9ubq-vVoVjio6F0w5qKVTNlJS-8VQ0WlHJ2orW3nHZElFRTZgSVFPieAVeMVYJD6AbLh2_QB-Pe-eXHifIoxn67CAEu4E4ZSMFF0QJNQ9eHgddijknaM029YNNe0OJOZhh1uaguDkobg5mmJMZZjeT352uTM0A_pl6Un_G3x_x1kZjH1Kfzf0vRiifU0rFOf8HviCScg</recordid><startdate>198010</startdate><enddate>198010</enddate><creator>Apel, K</creator><creator>Santel, H.J</creator><creator>Redlinger, T.E</creator><creator>Falk, H</creator><scope>FBQ</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>7X8</scope></search><sort><creationdate>198010</creationdate><title>protochlorophyllide holochrome of barley (Hordeum vulgare L.). 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Isolation and characterization of the NADPH: protochlorophyllide oxidoreductase</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1980-10</date><risdate>1980</risdate><volume>111</volume><issue>1</issue><spage>251</spage><epage>258</epage><pages>251-258</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>The NADPH:protochlorophyllide oxidoreductase of barley has been solubilized from etioplast membranes and purified to apparent homogeneity. The highest specific activity measured for the purified enzyme was 1.6 nmol chlorophyllide formed (mg protein-1) per flash. Electrophoretic analysis of the purified enzyme on sodium dodecylsulfate/polyacrylamide gels revealed only one polypeptide of Mr 36000. Durig glycerol gradient centrifugation the enzyme migrates as a low-molecular-weight component. It is proposed that each enzyme molecule contains only one polypeptide chain. Assuming a molecular weight of 36000 for the enzyme, it was calculated that two or three protochlorophyllide molecules are bound to each enzyme molecule.</abstract><cop>England</cop><pmid>7439188</pmid><doi>10.1111/j.1432-1033.1980.tb06100.x</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1980-10, Vol.111 (1), p.251-258 |
| issn | 0014-2956 1432-1033 |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Chlorophyll - analogs & derivatives Hordeum - enzymology Kinetics Microscopy, Electron Molecular Weight Oxidoreductases - isolation & purification Oxidoreductases - metabolism Oxidoreductases Acting on CH-CH Group Donors plant biochemistry plant physiology Plants - enzymology Protochlorophyllide - metabolism |
| title | protochlorophyllide holochrome of barley (Hordeum vulgare L.). Isolation and characterization of the NADPH: protochlorophyllide oxidoreductase |
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