Isolation and Preliminary Characterization of a Casein Kinase from Cauliflower Nuclei
A casein-type protein kinase has been isolated from cauliflower (Brassica cauliflora Gars.) nuclei and purified to a specific activity of 23,000 units/milligram of protein (1 unit is defined as the transfer of 1 picomole of 32Pi fromγ-[32P]ATP to substrate per minute at 28 C). The enzyme has a molec...
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| Veröffentlicht in: | Plant physiology (Bethesda) 1978-09, Vol.62 (3), p.434-437 |
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| container_end_page | 437 |
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| container_title | Plant physiology (Bethesda) |
| container_volume | 62 |
| creator | Murray, Michael G. Thomas J. Guilfoyle Key, Joe L. |
| description | A casein-type protein kinase has been isolated from cauliflower (Brassica cauliflora Gars.) nuclei and purified to a specific activity of 23,000 units/milligram of protein (1 unit is defined as the transfer of 1 picomole of 32Pi fromγ-[32P]ATP to substrate per minute at 28 C). The enzyme has a molecular weight of approximately 39,000 as judged by sucrose density gradient sedimentation. The casein kinase requires ATP as the phosphate donor and will phosphorylate casein and phosvitin, but not histones. The enzyme activity is not affected by cAMP or cGMP. The casein kinase appears to be analogous to casein kinases described in other plant and animal systems. |
| doi_str_mv | 10.1104/pp.62.3.434 |
| format | Article |
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Guilfoyle ; Key, Joe L.</creator><creatorcontrib>Murray, Michael G. ; Thomas J. Guilfoyle ; Key, Joe L.</creatorcontrib><description>A casein-type protein kinase has been isolated from cauliflower (Brassica cauliflora Gars.) nuclei and purified to a specific activity of 23,000 units/milligram of protein (1 unit is defined as the transfer of 1 picomole of 32Pi fromγ-[32P]ATP to substrate per minute at 28 C). The enzyme has a molecular weight of approximately 39,000 as judged by sucrose density gradient sedimentation. The casein kinase requires ATP as the phosphate donor and will phosphorylate casein and phosvitin, but not histones. The enzyme activity is not affected by cAMP or cGMP. The casein kinase appears to be analogous to casein kinases described in other plant and animal systems.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.62.3.434</identifier><identifier>PMID: 16660532</identifier><language>eng</language><publisher>United States: American Society of Plant Physiologists</publisher><subject>Cauliflower ; Cyclic nucleotides ; Enzymes ; Histones ; Nuclear proteins ; Phosphorylation ; Quaternary ammonium compounds ; RNA ; Soybeans ; Sulfates</subject><ispartof>Plant physiology (Bethesda), 1978-09, Vol.62 (3), p.434-437</ispartof><rights>Copyright 1978 The American Society of Plant Physiologists</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c432t-7789826af4983e21768650d91e2019e967c0daf25b93fb3f96e1eff51b475df53</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4265453$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4265453$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16660532$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Murray, Michael G.</creatorcontrib><creatorcontrib>Thomas J. Guilfoyle</creatorcontrib><creatorcontrib>Key, Joe L.</creatorcontrib><title>Isolation and Preliminary Characterization of a Casein Kinase from Cauliflower Nuclei</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>A casein-type protein kinase has been isolated from cauliflower (Brassica cauliflora Gars.) nuclei and purified to a specific activity of 23,000 units/milligram of protein (1 unit is defined as the transfer of 1 picomole of 32Pi fromγ-[32P]ATP to substrate per minute at 28 C). The enzyme has a molecular weight of approximately 39,000 as judged by sucrose density gradient sedimentation. The casein kinase requires ATP as the phosphate donor and will phosphorylate casein and phosvitin, but not histones. The enzyme activity is not affected by cAMP or cGMP. The casein kinase appears to be analogous to casein kinases described in other plant and animal systems.</description><subject>Cauliflower</subject><subject>Cyclic nucleotides</subject><subject>Enzymes</subject><subject>Histones</subject><subject>Nuclear proteins</subject><subject>Phosphorylation</subject><subject>Quaternary ammonium compounds</subject><subject>RNA</subject><subject>Soybeans</subject><subject>Sulfates</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><recordid>eNpV0U1PGzEQBmCrompS2lOvCO2thyrB32tfkFDEl4igh3K2nN0xMfKuF3u3iP56XCWi5WTL8-j12IPQN4KXhGB-MgxLSZdsyRn_gOZEMLqggqsDNMe47LFSeoY-5_yIMSaM8E9oRqSUuMA5ur_OMdjRx76yfVv9TBB853ubXqrV1ibbjJD8nx2IrrLVymbwfXVTTIbKpdiVoyl4F-IzpOp2agL4L-ijsyHD1_16iO4vzn-trhbru8vr1dl60XBGx0VdK62otI5rxYCSWiopcKsJUEw0aFk3uLWOio1mbsOclkDAOUE2vBatE-wQne5yh2nTQdtAPyYbzJB8V15govXmfaX3W_MQfxuCNSWclIDv-4AUnybIo-l8biAE20OcsqkZ40qpWhf5YyebFHNO4N5uIdj8nYMZBiOpYabMoejj_xv7Z_cfX8DRDjzmMaa3OqdScMHYK6RfjeQ</recordid><startdate>19780901</startdate><enddate>19780901</enddate><creator>Murray, Michael G.</creator><creator>Thomas J. Guilfoyle</creator><creator>Key, Joe L.</creator><general>American Society of Plant Physiologists</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19780901</creationdate><title>Isolation and Preliminary Characterization of a Casein Kinase from Cauliflower Nuclei</title><author>Murray, Michael G. ; Thomas J. Guilfoyle ; Key, Joe L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c432t-7789826af4983e21768650d91e2019e967c0daf25b93fb3f96e1eff51b475df53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Cauliflower</topic><topic>Cyclic nucleotides</topic><topic>Enzymes</topic><topic>Histones</topic><topic>Nuclear proteins</topic><topic>Phosphorylation</topic><topic>Quaternary ammonium compounds</topic><topic>RNA</topic><topic>Soybeans</topic><topic>Sulfates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Murray, Michael G.</creatorcontrib><creatorcontrib>Thomas J. Guilfoyle</creatorcontrib><creatorcontrib>Key, Joe L.</creatorcontrib><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>Murray, Michael G.</au><au>Thomas J. Guilfoyle</au><au>Key, Joe L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and Preliminary Characterization of a Casein Kinase from Cauliflower Nuclei</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1978-09-01</date><risdate>1978</risdate><volume>62</volume><issue>3</issue><spage>434</spage><epage>437</epage><pages>434-437</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><abstract>A casein-type protein kinase has been isolated from cauliflower (Brassica cauliflora Gars.) nuclei and purified to a specific activity of 23,000 units/milligram of protein (1 unit is defined as the transfer of 1 picomole of 32Pi fromγ-[32P]ATP to substrate per minute at 28 C). The enzyme has a molecular weight of approximately 39,000 as judged by sucrose density gradient sedimentation. The casein kinase requires ATP as the phosphate donor and will phosphorylate casein and phosvitin, but not histones. The enzyme activity is not affected by cAMP or cGMP. The casein kinase appears to be analogous to casein kinases described in other plant and animal systems.</abstract><cop>United States</cop><pub>American Society of Plant Physiologists</pub><pmid>16660532</pmid><doi>10.1104/pp.62.3.434</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Plant physiology (Bethesda), 1978-09, Vol.62 (3), p.434-437 |
| issn | 0032-0889 1532-2548 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_733488879 |
| source | Alma/SFX Local Collection; JSTOR; EZB Electronic Journals Library |
| subjects | Cauliflower Cyclic nucleotides Enzymes Histones Nuclear proteins Phosphorylation Quaternary ammonium compounds RNA Soybeans Sulfates |
| title | Isolation and Preliminary Characterization of a Casein Kinase from Cauliflower Nuclei |
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