Protein phosphorylation as a mechanism for regulation of spinach leaf sucrose-phosphate synthase activity
Studies were conducted to determine whether protein phosphorylation may be a mechanism for regulation of spinach ( Spinacia oleracea L.) leaf sucrose-phosphate synthase (SPS), shown previously to be light-dark regulated by some type of covalent modification. Radioactive phosphate was incorporated in...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1989-05, Vol.270 (2), p.681-690 |
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| creator | Huber, Joan L.A. Huber, Steven C. Nielsen, Tom Hamborg |
| description | Studies were conducted to determine whether protein phosphorylation may be a mechanism for regulation of spinach (
Spinacia oleracea L.) leaf sucrose-phosphate synthase (SPS), shown previously to be light-dark regulated by some type of covalent modification. Radioactive phosphate was incorporated into the 120-kDa subunit of SPS during labeling of excised leaves with [
32P]
P
i, as shown by immunoprecipitation and denaturing gel electrophoresis of the enzyme. Conditions which activated the enzyme (illumination of leaves or mannose treatment of leaf discs in darkness) reduced the incorporation of radiolabel into SPS in the
in vivo system. The partially purified SPS protein could also be phosphorylated
in vitro using [γ-
32P]ATP. In the
in vitro system, the incorporation of radiolabel into the 120-kDa subunit of SPS was dependent on time and magnesium concentration, and was closely paralleled by inactivation of the enzyme. These results provide the first evidence to establish protein phosphorylation as a mechanism for the covalent regulation of SPS activity. |
| doi_str_mv | 10.1016/0003-9861(89)90551-1 |
| format | Article |
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Spinacia oleracea L.) leaf sucrose-phosphate synthase (SPS), shown previously to be light-dark regulated by some type of covalent modification. Radioactive phosphate was incorporated into the 120-kDa subunit of SPS during labeling of excised leaves with [
32P]
P
i, as shown by immunoprecipitation and denaturing gel electrophoresis of the enzyme. Conditions which activated the enzyme (illumination of leaves or mannose treatment of leaf discs in darkness) reduced the incorporation of radiolabel into SPS in the
in vivo system. The partially purified SPS protein could also be phosphorylated
in vitro using [γ-
32P]ATP. In the
in vitro system, the incorporation of radiolabel into the 120-kDa subunit of SPS was dependent on time and magnesium concentration, and was closely paralleled by inactivation of the enzyme. These results provide the first evidence to establish protein phosphorylation as a mechanism for the covalent regulation of SPS activity.</description><identifier>ISSN: 0003-9861</identifier><identifier>ISSN: 0079-2241</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(89)90551-1</identifier><identifier>PMID: 2523212</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>550201 - Biochemistry- Tracer Techniques ; ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Adenosine Triphosphate - pharmacology ; ALKALINE EARTH METALS ; Analytical, structural and metabolic biochemistry ; ATP ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; BETA-MINUS DECAY RADIOISOTOPES ; Biological and medical sciences ; CHEMICAL REACTIONS ; Chloroplasts - enzymology ; DAYS LIVING RADIOISOTOPES ; Electrophoresis, Polyacrylamide Gel ; ELEMENTS ; Enzyme Activation - drug effects ; ENZYME ACTIVITY ; ENZYMES ; Enzymes and enzyme inhibitors ; ENZYMIC ACTIVITY ; FEUILLE ; FOOD ; FOSFATOS ; FOSFORILACION ; Fundamental and applied biological sciences. Psychology ; Glucosyltransferases - antagonists & inhibitors ; Glucosyltransferases - metabolism ; GLYCOSYL TRANSFERASES ; HOJAS ; IN VITRO ; ISOTOPE APPLICATIONS ; ISOTOPES ; LEAVES ; LIGASA ; LIGASE ; LIGASES ; Light ; LIGHT NUCLEI ; MAGNESIUM ; Magnesium - pharmacology ; MAGNOLIOPHYTA ; MAGNOLIOPSIDA ; Mannose - pharmacology ; METALS ; NUCLEI ; NUCLEOTIDES ; ODD-ODD NUCLEI ; ORGANIC COMPOUNDS ; PHOSPHATE ; PHOSPHATES ; PHOSPHORUS 32 ; PHOSPHORUS ISOTOPES ; PHOSPHORUS-GROUP TRANSFERASES ; PHOSPHORYLATION ; PHOSPHOTRANSFERASES ; Plant Proteins - metabolism ; PLANTS ; PROTEINS ; RADIOISOTOPES ; SPINACH ; SPINACIA OLERACEA ; SUCROSA ; SUCROSE ; sucrose-phosphate synthase ; TIME DEPENDENCE ; TRACER TECHNIQUES ; TRANSFERASES ; VEGETABLES</subject><ispartof>Archives of biochemistry and biophysics, 1989-05, Vol.270 (2), p.681-690</ispartof><rights>1989</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c530t-dac8f4d8d58d6b2b0612b5d30830ad561304ea6798e9076cdf1396437968e0563</citedby><cites>FETCH-LOGICAL-c530t-dac8f4d8d58d6b2b0612b5d30830ad561304ea6798e9076cdf1396437968e0563</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(89)90551-1$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19298670$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2523212$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/7027054$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Huber, Joan L.A.</creatorcontrib><creatorcontrib>Huber, Steven C.</creatorcontrib><creatorcontrib>Nielsen, Tom Hamborg</creatorcontrib><title>Protein phosphorylation as a mechanism for regulation of spinach leaf sucrose-phosphate synthase activity</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Studies were conducted to determine whether protein phosphorylation may be a mechanism for regulation of spinach (
Spinacia oleracea L.) leaf sucrose-phosphate synthase (SPS), shown previously to be light-dark regulated by some type of covalent modification. Radioactive phosphate was incorporated into the 120-kDa subunit of SPS during labeling of excised leaves with [
32P]
P
i, as shown by immunoprecipitation and denaturing gel electrophoresis of the enzyme. Conditions which activated the enzyme (illumination of leaves or mannose treatment of leaf discs in darkness) reduced the incorporation of radiolabel into SPS in the
in vivo system. The partially purified SPS protein could also be phosphorylated
in vitro using [γ-
32P]ATP. In the
in vitro system, the incorporation of radiolabel into the 120-kDa subunit of SPS was dependent on time and magnesium concentration, and was closely paralleled by inactivation of the enzyme. These results provide the first evidence to establish protein phosphorylation as a mechanism for the covalent regulation of SPS activity.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Adenosine Triphosphate - pharmacology</subject><subject>ALKALINE EARTH METALS</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>ATP</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BETA-MINUS DECAY RADIOISOTOPES</subject><subject>Biological and medical sciences</subject><subject>CHEMICAL REACTIONS</subject><subject>Chloroplasts - enzymology</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>ELEMENTS</subject><subject>Enzyme Activation - drug effects</subject><subject>ENZYME ACTIVITY</subject><subject>ENZYMES</subject><subject>Enzymes and enzyme inhibitors</subject><subject>ENZYMIC ACTIVITY</subject><subject>FEUILLE</subject><subject>FOOD</subject><subject>FOSFATOS</subject><subject>FOSFORILACION</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucosyltransferases - antagonists & inhibitors</subject><subject>Glucosyltransferases - metabolism</subject><subject>GLYCOSYL TRANSFERASES</subject><subject>HOJAS</subject><subject>IN VITRO</subject><subject>ISOTOPE APPLICATIONS</subject><subject>ISOTOPES</subject><subject>LEAVES</subject><subject>LIGASA</subject><subject>LIGASE</subject><subject>LIGASES</subject><subject>Light</subject><subject>LIGHT NUCLEI</subject><subject>MAGNESIUM</subject><subject>Magnesium - pharmacology</subject><subject>MAGNOLIOPHYTA</subject><subject>MAGNOLIOPSIDA</subject><subject>Mannose - pharmacology</subject><subject>METALS</subject><subject>NUCLEI</subject><subject>NUCLEOTIDES</subject><subject>ODD-ODD NUCLEI</subject><subject>ORGANIC COMPOUNDS</subject><subject>PHOSPHATE</subject><subject>PHOSPHATES</subject><subject>PHOSPHORUS 32</subject><subject>PHOSPHORUS ISOTOPES</subject><subject>PHOSPHORUS-GROUP TRANSFERASES</subject><subject>PHOSPHORYLATION</subject><subject>PHOSPHOTRANSFERASES</subject><subject>Plant Proteins - metabolism</subject><subject>PLANTS</subject><subject>PROTEINS</subject><subject>RADIOISOTOPES</subject><subject>SPINACH</subject><subject>SPINACIA OLERACEA</subject><subject>SUCROSA</subject><subject>SUCROSE</subject><subject>sucrose-phosphate synthase</subject><subject>TIME DEPENDENCE</subject><subject>TRACER TECHNIQUES</subject><subject>TRANSFERASES</subject><subject>VEGETABLES</subject><issn>0003-9861</issn><issn>0079-2241</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU-L1TAUxYMo43P0C4hCERRdVG-aJk02ggz-gwEFnXXIS2_nRdrkTZIOvG9vasu400UI4fzu4eYcQp5ReEuBincAwGolBX0t1RsFnNOa3iM7CkrUwGR7n-zukIfkUUq_AChtRXNGzhresIY2O-K-x5DR-ep4CKmceBpNdsFXJlWmmtAejHdpqoYQq4jX86aGoUpH5409VCOa8phtDAnr1cVkrNLJ54NJWBmb3a3Lp8fkwWDGhE-2-5xcffr48-JLffnt89eLD5e15Qxy3Rsrh7aXPZe92Dd7ELTZ856BZGB6LiiDFo3olEQFnbD9QJkSLeuUkAhcsHPyYvUNKTudrMvlEzZ4jzbrDpoOeFugVyt0jOFmxpT15JLFcTQew5x0xzvBmRT_BSlvOFeKFrBdwSWIFHHQx-gmE0-agl760ksZeilDS6X_9KWXseeb_7yfsL8b2goq-stNN8macYjGW5f-equmOHZQuKcrN5igzXUszNUPqahgUhXx_Spiyf3WYVxiQW-xd3FJpQ_u31v-BnMCuao</recordid><startdate>19890501</startdate><enddate>19890501</enddate><creator>Huber, Joan L.A.</creator><creator>Huber, Steven C.</creator><creator>Nielsen, Tom Hamborg</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19890501</creationdate><title>Protein phosphorylation as a mechanism for regulation of spinach leaf sucrose-phosphate synthase activity</title><author>Huber, Joan L.A. ; Huber, Steven C. ; Nielsen, Tom Hamborg</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c530t-dac8f4d8d58d6b2b0612b5d30830ad561304ea6798e9076cdf1396437968e0563</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Adenosine Triphosphate - pharmacology</topic><topic>ALKALINE EARTH METALS</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>ATP</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BETA-MINUS DECAY RADIOISOTOPES</topic><topic>Biological and medical sciences</topic><topic>CHEMICAL REACTIONS</topic><topic>Chloroplasts - enzymology</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>ELEMENTS</topic><topic>Enzyme Activation - drug effects</topic><topic>ENZYME ACTIVITY</topic><topic>ENZYMES</topic><topic>Enzymes and enzyme inhibitors</topic><topic>ENZYMIC ACTIVITY</topic><topic>FEUILLE</topic><topic>FOOD</topic><topic>FOSFATOS</topic><topic>FOSFORILACION</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glucosyltransferases - antagonists & inhibitors</topic><topic>Glucosyltransferases - metabolism</topic><topic>GLYCOSYL TRANSFERASES</topic><topic>HOJAS</topic><topic>IN VITRO</topic><topic>ISOTOPE APPLICATIONS</topic><topic>ISOTOPES</topic><topic>LEAVES</topic><topic>LIGASA</topic><topic>LIGASE</topic><topic>LIGASES</topic><topic>Light</topic><topic>LIGHT NUCLEI</topic><topic>MAGNESIUM</topic><topic>Magnesium - pharmacology</topic><topic>MAGNOLIOPHYTA</topic><topic>MAGNOLIOPSIDA</topic><topic>Mannose - pharmacology</topic><topic>METALS</topic><topic>NUCLEI</topic><topic>NUCLEOTIDES</topic><topic>ODD-ODD NUCLEI</topic><topic>ORGANIC COMPOUNDS</topic><topic>PHOSPHATE</topic><topic>PHOSPHATES</topic><topic>PHOSPHORUS 32</topic><topic>PHOSPHORUS ISOTOPES</topic><topic>PHOSPHORUS-GROUP TRANSFERASES</topic><topic>PHOSPHORYLATION</topic><topic>PHOSPHOTRANSFERASES</topic><topic>Plant Proteins - metabolism</topic><topic>PLANTS</topic><topic>PROTEINS</topic><topic>RADIOISOTOPES</topic><topic>SPINACH</topic><topic>SPINACIA OLERACEA</topic><topic>SUCROSA</topic><topic>SUCROSE</topic><topic>sucrose-phosphate synthase</topic><topic>TIME DEPENDENCE</topic><topic>TRACER TECHNIQUES</topic><topic>TRANSFERASES</topic><topic>VEGETABLES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Huber, Joan L.A.</creatorcontrib><creatorcontrib>Huber, Steven C.</creatorcontrib><creatorcontrib>Nielsen, Tom Hamborg</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huber, Joan L.A.</au><au>Huber, Steven C.</au><au>Nielsen, Tom Hamborg</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein phosphorylation as a mechanism for regulation of spinach leaf sucrose-phosphate synthase activity</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1989-05-01</date><risdate>1989</risdate><volume>270</volume><issue>2</issue><spage>681</spage><epage>690</epage><pages>681-690</pages><issn>0003-9861</issn><issn>0079-2241</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>Studies were conducted to determine whether protein phosphorylation may be a mechanism for regulation of spinach (
Spinacia oleracea L.) leaf sucrose-phosphate synthase (SPS), shown previously to be light-dark regulated by some type of covalent modification. Radioactive phosphate was incorporated into the 120-kDa subunit of SPS during labeling of excised leaves with [
32P]
P
i, as shown by immunoprecipitation and denaturing gel electrophoresis of the enzyme. Conditions which activated the enzyme (illumination of leaves or mannose treatment of leaf discs in darkness) reduced the incorporation of radiolabel into SPS in the
in vivo system. The partially purified SPS protein could also be phosphorylated
in vitro using [γ-
32P]ATP. In the
in vitro system, the incorporation of radiolabel into the 120-kDa subunit of SPS was dependent on time and magnesium concentration, and was closely paralleled by inactivation of the enzyme. These results provide the first evidence to establish protein phosphorylation as a mechanism for the covalent regulation of SPS activity.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2523212</pmid><doi>10.1016/0003-9861(89)90551-1</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Archives of biochemistry and biophysics, 1989-05, Vol.270 (2), p.681-690 |
| issn | 0003-9861 0079-2241 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75765386 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | 550201 - Biochemistry- Tracer Techniques ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Adenosine Triphosphate - pharmacology ALKALINE EARTH METALS Analytical, structural and metabolic biochemistry ATP BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES BETA-MINUS DECAY RADIOISOTOPES Biological and medical sciences CHEMICAL REACTIONS Chloroplasts - enzymology DAYS LIVING RADIOISOTOPES Electrophoresis, Polyacrylamide Gel ELEMENTS Enzyme Activation - drug effects ENZYME ACTIVITY ENZYMES Enzymes and enzyme inhibitors ENZYMIC ACTIVITY FEUILLE FOOD FOSFATOS FOSFORILACION Fundamental and applied biological sciences. Psychology Glucosyltransferases - antagonists & inhibitors Glucosyltransferases - metabolism GLYCOSYL TRANSFERASES HOJAS IN VITRO ISOTOPE APPLICATIONS ISOTOPES LEAVES LIGASA LIGASE LIGASES Light LIGHT NUCLEI MAGNESIUM Magnesium - pharmacology MAGNOLIOPHYTA MAGNOLIOPSIDA Mannose - pharmacology METALS NUCLEI NUCLEOTIDES ODD-ODD NUCLEI ORGANIC COMPOUNDS PHOSPHATE PHOSPHATES PHOSPHORUS 32 PHOSPHORUS ISOTOPES PHOSPHORUS-GROUP TRANSFERASES PHOSPHORYLATION PHOSPHOTRANSFERASES Plant Proteins - metabolism PLANTS PROTEINS RADIOISOTOPES SPINACH SPINACIA OLERACEA SUCROSA SUCROSE sucrose-phosphate synthase TIME DEPENDENCE TRACER TECHNIQUES TRANSFERASES VEGETABLES |
| title | Protein phosphorylation as a mechanism for regulation of spinach leaf sucrose-phosphate synthase activity |
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