Studies on nucleotidases in plants: Reversible denaturation of the crystalline mung bean nucleotide pyrophosphatase and the effect of adenylates on the native and renatured enzyme
The crystalline mung bean nucleotide pyrophosphatase was inhibited nonlinearly by AMP, one of the products of the reaction. The partially inactive enzyme was specifically reactivated by ADP, and V at maximal activation was the same as that of the native enzyme. ATP was a linear, noncompetitive inhib...
Gespeichert in:
| Veröffentlicht in: | Archives of biochemistry and biophysics 1974-01, Vol.164 (1), p.156-164 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 164 |
|---|---|
| container_issue | 1 |
| container_start_page | 156 |
| container_title | Archives of biochemistry and biophysics |
| container_volume | 164 |
| creator | Balakrishnan, C.V. Ravindranath, S.D. Rao, N.Appaji |
| description | The crystalline mung bean nucleotide pyrophosphatase was inhibited nonlinearly by AMP, one of the products of the reaction. The partially inactive enzyme was specifically reactivated by ADP, and
V at maximal activation was the same as that of the native enzyme. ATP was a linear, noncompetitive inhibitor. The kinetic evidence suggested that ADP and ATP might not be reacting at the same site as AMP. The electrophoretic mobility of the enzyme was increased by AMP, whereas ADP and ATP were without effect.
The enzyme was denatured on treatment with urea or guanidine hydrochloride. The renatured and the native enzyme had the same pH (9.4) and temperature (49 °C) optimum. The
K
m
(0.2 m
m) and
V (3.2) of the native enzyme increased on renaturation to 1.8 m
m and 8.0, respectively. In addition, renaturation resulted in desensitization of the enzyme to inhibition by low concentrations of AMP. Renaturation did not affect the reactivation of the apoenzyme by Zn
2+. |
| doi_str_mv | 10.1016/0003-9861(74)90017-4 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_82555952</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0003986174900174</els_id><sourcerecordid>82555952</sourcerecordid><originalsourceid>FETCH-LOGICAL-e285t-1a2c4ae1a08653cd588ce9f17f6c469419fbe8d1a6402e784e02c9d232e30a2c3</originalsourceid><addsrcrecordid>eNpNkd2K1TAUhYMo45nRN1DMlYwX1fy1TeZCkME_GBAc5zrkJLtzIm1ak_RAfS1f0HR6EK8C2d9aO1kLoReUvKWENu8IIbxSsqGXrXijCKFtJR6hHSWqqQiX4jHa_UOeovOUfhaGioadoTMhmOKi3aE_t3l2HhIeAw6z7WHM3plULnzAU29CTlf4OxwhJr_vATsIJs_RZF8EY4fzAbCNS8qm730APMzhHu_B_OcGeFriOB3GNB1MLt7YBPcghK4Dm1cbU3yX3uTtIeusrPHHDY3bTnAYwu9lgGfoSWf6BM9P5wW6-_Txx_WX6ubb56_XH24qYLLOFTXMCgPUENnU3LpaSguqo23XWNEoQVW3B-moaQRh0EoBhFnlGGfASdHyC_R6853i-GuGlPXgk4W-pALjnLRkdV2rmhXw5Qmc9wM4PUU_mLjoU8pl_mqbd2bU5j76pO9uGaGccCoVbZtCvN8IKP85eog6WQ_BgvOxRKTd6DUleu1dr6XqtVTdCv3Quxb8L1rfoVk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>82555952</pqid></control><display><type>article</type><title>Studies on nucleotidases in plants: Reversible denaturation of the crystalline mung bean nucleotide pyrophosphatase and the effect of adenylates on the native and renatured enzyme</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Balakrishnan, C.V. ; Ravindranath, S.D. ; Rao, N.Appaji</creator><creatorcontrib>Balakrishnan, C.V. ; Ravindranath, S.D. ; Rao, N.Appaji</creatorcontrib><description>The crystalline mung bean nucleotide pyrophosphatase was inhibited nonlinearly by AMP, one of the products of the reaction. The partially inactive enzyme was specifically reactivated by ADP, and
V at maximal activation was the same as that of the native enzyme. ATP was a linear, noncompetitive inhibitor. The kinetic evidence suggested that ADP and ATP might not be reacting at the same site as AMP. The electrophoretic mobility of the enzyme was increased by AMP, whereas ADP and ATP were without effect.
The enzyme was denatured on treatment with urea or guanidine hydrochloride. The renatured and the native enzyme had the same pH (9.4) and temperature (49 °C) optimum. The
K
m
(0.2 m
m) and
V (3.2) of the native enzyme increased on renaturation to 1.8 m
m and 8.0, respectively. In addition, renaturation resulted in desensitization of the enzyme to inhibition by low concentrations of AMP. Renaturation did not affect the reactivation of the apoenzyme by Zn
2+.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(74)90017-4</identifier><identifier>PMID: 4429347</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenine Nucleotides - pharmacology ; Adenosine Diphosphate - pharmacology ; Adenosine Monophosphate - pharmacology ; Adenosine Triphosphate - pharmacology ; Binding Sites ; Chromatography, Paper ; Electrophoresis, Polyacrylamide Gel ; Flavin Mononucleotide - pharmacology ; Flavin-Adenine Dinucleotide - pharmacology ; Guanidines ; horticultural crops ; Hydrogen-Ion Concentration ; Kinetics ; Nucleotidases - metabolism ; plant biochemistry ; plant physiology ; Plants - drug effects ; Plants - enzymology ; Protein Binding ; Protein Denaturation ; Pyrophosphatases - metabolism ; Sodium Dodecyl Sulfate ; Spectrometry, Fluorescence ; Temperature ; Time Factors ; Urea</subject><ispartof>Archives of biochemistry and biophysics, 1974-01, Vol.164 (1), p.156-164</ispartof><rights>1974</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(74)90017-4$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4429347$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Balakrishnan, C.V.</creatorcontrib><creatorcontrib>Ravindranath, S.D.</creatorcontrib><creatorcontrib>Rao, N.Appaji</creatorcontrib><title>Studies on nucleotidases in plants: Reversible denaturation of the crystalline mung bean nucleotide pyrophosphatase and the effect of adenylates on the native and renatured enzyme</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The crystalline mung bean nucleotide pyrophosphatase was inhibited nonlinearly by AMP, one of the products of the reaction. The partially inactive enzyme was specifically reactivated by ADP, and
V at maximal activation was the same as that of the native enzyme. ATP was a linear, noncompetitive inhibitor. The kinetic evidence suggested that ADP and ATP might not be reacting at the same site as AMP. The electrophoretic mobility of the enzyme was increased by AMP, whereas ADP and ATP were without effect.
The enzyme was denatured on treatment with urea or guanidine hydrochloride. The renatured and the native enzyme had the same pH (9.4) and temperature (49 °C) optimum. The
K
m
(0.2 m
m) and
V (3.2) of the native enzyme increased on renaturation to 1.8 m
m and 8.0, respectively. In addition, renaturation resulted in desensitization of the enzyme to inhibition by low concentrations of AMP. Renaturation did not affect the reactivation of the apoenzyme by Zn
2+.</description><subject>Adenine Nucleotides - pharmacology</subject><subject>Adenosine Diphosphate - pharmacology</subject><subject>Adenosine Monophosphate - pharmacology</subject><subject>Adenosine Triphosphate - pharmacology</subject><subject>Binding Sites</subject><subject>Chromatography, Paper</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Flavin Mononucleotide - pharmacology</subject><subject>Flavin-Adenine Dinucleotide - pharmacology</subject><subject>Guanidines</subject><subject>horticultural crops</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Nucleotidases - metabolism</subject><subject>plant biochemistry</subject><subject>plant physiology</subject><subject>Plants - drug effects</subject><subject>Plants - enzymology</subject><subject>Protein Binding</subject><subject>Protein Denaturation</subject><subject>Pyrophosphatases - metabolism</subject><subject>Sodium Dodecyl Sulfate</subject><subject>Spectrometry, Fluorescence</subject><subject>Temperature</subject><subject>Time Factors</subject><subject>Urea</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkd2K1TAUhYMo45nRN1DMlYwX1fy1TeZCkME_GBAc5zrkJLtzIm1ak_RAfS1f0HR6EK8C2d9aO1kLoReUvKWENu8IIbxSsqGXrXijCKFtJR6hHSWqqQiX4jHa_UOeovOUfhaGioadoTMhmOKi3aE_t3l2HhIeAw6z7WHM3plULnzAU29CTlf4OxwhJr_vATsIJs_RZF8EY4fzAbCNS8qm730APMzhHu_B_OcGeFriOB3GNB1MLt7YBPcghK4Dm1cbU3yX3uTtIeusrPHHDY3bTnAYwu9lgGfoSWf6BM9P5wW6-_Txx_WX6ubb56_XH24qYLLOFTXMCgPUENnU3LpaSguqo23XWNEoQVW3B-moaQRh0EoBhFnlGGfASdHyC_R6853i-GuGlPXgk4W-pALjnLRkdV2rmhXw5Qmc9wM4PUU_mLjoU8pl_mqbd2bU5j76pO9uGaGccCoVbZtCvN8IKP85eog6WQ_BgvOxRKTd6DUleu1dr6XqtVTdCv3Quxb8L1rfoVk</recordid><startdate>19740101</startdate><enddate>19740101</enddate><creator>Balakrishnan, C.V.</creator><creator>Ravindranath, S.D.</creator><creator>Rao, N.Appaji</creator><general>Elsevier Inc</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19740101</creationdate><title>Studies on nucleotidases in plants: Reversible denaturation of the crystalline mung bean nucleotide pyrophosphatase and the effect of adenylates on the native and renatured enzyme</title><author>Balakrishnan, C.V. ; Ravindranath, S.D. ; Rao, N.Appaji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e285t-1a2c4ae1a08653cd588ce9f17f6c469419fbe8d1a6402e784e02c9d232e30a2c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1974</creationdate><topic>Adenine Nucleotides - pharmacology</topic><topic>Adenosine Diphosphate - pharmacology</topic><topic>Adenosine Monophosphate - pharmacology</topic><topic>Adenosine Triphosphate - pharmacology</topic><topic>Binding Sites</topic><topic>Chromatography, Paper</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Flavin Mononucleotide - pharmacology</topic><topic>Flavin-Adenine Dinucleotide - pharmacology</topic><topic>Guanidines</topic><topic>horticultural crops</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Nucleotidases - metabolism</topic><topic>plant biochemistry</topic><topic>plant physiology</topic><topic>Plants - drug effects</topic><topic>Plants - enzymology</topic><topic>Protein Binding</topic><topic>Protein Denaturation</topic><topic>Pyrophosphatases - metabolism</topic><topic>Sodium Dodecyl Sulfate</topic><topic>Spectrometry, Fluorescence</topic><topic>Temperature</topic><topic>Time Factors</topic><topic>Urea</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Balakrishnan, C.V.</creatorcontrib><creatorcontrib>Ravindranath, S.D.</creatorcontrib><creatorcontrib>Rao, N.Appaji</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Balakrishnan, C.V.</au><au>Ravindranath, S.D.</au><au>Rao, N.Appaji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies on nucleotidases in plants: Reversible denaturation of the crystalline mung bean nucleotide pyrophosphatase and the effect of adenylates on the native and renatured enzyme</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1974-01-01</date><risdate>1974</risdate><volume>164</volume><issue>1</issue><spage>156</spage><epage>164</epage><pages>156-164</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The crystalline mung bean nucleotide pyrophosphatase was inhibited nonlinearly by AMP, one of the products of the reaction. The partially inactive enzyme was specifically reactivated by ADP, and
V at maximal activation was the same as that of the native enzyme. ATP was a linear, noncompetitive inhibitor. The kinetic evidence suggested that ADP and ATP might not be reacting at the same site as AMP. The electrophoretic mobility of the enzyme was increased by AMP, whereas ADP and ATP were without effect.
The enzyme was denatured on treatment with urea or guanidine hydrochloride. The renatured and the native enzyme had the same pH (9.4) and temperature (49 °C) optimum. The
K
m
(0.2 m
m) and
V (3.2) of the native enzyme increased on renaturation to 1.8 m
m and 8.0, respectively. In addition, renaturation resulted in desensitization of the enzyme to inhibition by low concentrations of AMP. Renaturation did not affect the reactivation of the apoenzyme by Zn
2+.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4429347</pmid><doi>10.1016/0003-9861(74)90017-4</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1974-01, Vol.164 (1), p.156-164 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_82555952 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Adenine Nucleotides - pharmacology Adenosine Diphosphate - pharmacology Adenosine Monophosphate - pharmacology Adenosine Triphosphate - pharmacology Binding Sites Chromatography, Paper Electrophoresis, Polyacrylamide Gel Flavin Mononucleotide - pharmacology Flavin-Adenine Dinucleotide - pharmacology Guanidines horticultural crops Hydrogen-Ion Concentration Kinetics Nucleotidases - metabolism plant biochemistry plant physiology Plants - drug effects Plants - enzymology Protein Binding Protein Denaturation Pyrophosphatases - metabolism Sodium Dodecyl Sulfate Spectrometry, Fluorescence Temperature Time Factors Urea |
| title | Studies on nucleotidases in plants: Reversible denaturation of the crystalline mung bean nucleotide pyrophosphatase and the effect of adenylates on the native and renatured enzyme |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T15%3A29%3A43IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Studies%20on%20nucleotidases%20in%20plants:%20Reversible%20denaturation%20of%20the%20crystalline%20mung%20bean%20nucleotide%20pyrophosphatase%20and%20the%20effect%20of%20adenylates%20on%20the%20native%20and%20renatured%20enzyme&rft.jtitle=Archives%20of%20biochemistry%20and%20biophysics&rft.au=Balakrishnan,%20C.V.&rft.date=1974-01-01&rft.volume=164&rft.issue=1&rft.spage=156&rft.epage=164&rft.pages=156-164&rft.issn=0003-9861&rft.eissn=1096-0384&rft_id=info:doi/10.1016/0003-9861(74)90017-4&rft_dat=%3Cproquest_pubme%3E82555952%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=82555952&rft_id=info:pmid/4429347&rft_els_id=0003986174900174&rfr_iscdi=true |