Phosphorylation of casein and lysozyme by phosphorus oxychloride
Casein and lysozyme were phosphorylated by phosphorus oxychloride at pH 6-8 and 3-20 degree C. Up to 7.4 and 6.2 mol of phosphate/mol of protein were covalently attached to casein and lysozyme, respectively. super(31)P NMR spectral data and pH stability studies of the phosphate residues indicated th...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 1983-03, Vol.31 (2), p.379-387 |
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| container_end_page | 387 |
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| container_issue | 2 |
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| container_title | Journal of agricultural and food chemistry |
| container_volume | 31 |
| creator | Matheis, Guenter Penner, Michael H Feeney, Robert E Whitaker, John R |
| description | Casein and lysozyme were phosphorylated by phosphorus oxychloride at pH 6-8 and 3-20 degree C. Up to 7.4 and 6.2 mol of phosphate/mol of protein were covalently attached to casein and lysozyme, respectively. super(31)P NMR spectral data and pH stability studies of the phosphate residues indicated that in phosphorylated casein, the phosphate was exclusively bound to hydroxyl oxygen as monophosphate and diphosphate. The phosphate linkages were stable at pH 2.0-8.5. In contrast, the majority of the phosphate in phosphorylated lysozyme appeared to be bound to nitrogen. In addition to mono- and diphosphate, triphosphate bonds were present. Gel electrophoresis in the presence of sodium dodecyl sulfate and urea indicated that protein cross-linking occurred during phosphorylation. |
| doi_str_mv | 10.1021/jf00116a049 |
| format | Article |
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Up to 7.4 and 6.2 mol of phosphate/mol of protein were covalently attached to casein and lysozyme, respectively. super(31)P NMR spectral data and pH stability studies of the phosphate residues indicated that in phosphorylated casein, the phosphate was exclusively bound to hydroxyl oxygen as monophosphate and diphosphate. The phosphate linkages were stable at pH 2.0-8.5. In contrast, the majority of the phosphate in phosphorylated lysozyme appeared to be bound to nitrogen. In addition to mono- and diphosphate, triphosphate bonds were present. Gel electrophoresis in the presence of sodium dodecyl sulfate and urea indicated that protein cross-linking occurred during phosphorylation.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf00116a049</identifier><identifier>PMID: 6853861</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>casein ; Caseins - metabolism ; Dietary Proteins - metabolism ; Digestion ; lysozyme ; Muramidase - metabolism ; Phosphorus ; Phosphorus Compounds ; phosphorus oxychloride ; Phosphorylation</subject><ispartof>Journal of agricultural and food chemistry, 1983-03, Vol.31 (2), p.379-387</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a385t-78b2882ab36905c7059c0c52586b3dde0d35de5edbd39f26aaa0ab882714775c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf00116a049$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf00116a049$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6853861$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Matheis, Guenter</creatorcontrib><creatorcontrib>Penner, Michael H</creatorcontrib><creatorcontrib>Feeney, Robert E</creatorcontrib><creatorcontrib>Whitaker, John R</creatorcontrib><title>Phosphorylation of casein and lysozyme by phosphorus oxychloride</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Casein and lysozyme were phosphorylated by phosphorus oxychloride at pH 6-8 and 3-20 degree C. Up to 7.4 and 6.2 mol of phosphate/mol of protein were covalently attached to casein and lysozyme, respectively. super(31)P NMR spectral data and pH stability studies of the phosphate residues indicated that in phosphorylated casein, the phosphate was exclusively bound to hydroxyl oxygen as monophosphate and diphosphate. The phosphate linkages were stable at pH 2.0-8.5. In contrast, the majority of the phosphate in phosphorylated lysozyme appeared to be bound to nitrogen. In addition to mono- and diphosphate, triphosphate bonds were present. Gel electrophoresis in the presence of sodium dodecyl sulfate and urea indicated that protein cross-linking occurred during phosphorylation.</description><subject>casein</subject><subject>Caseins - metabolism</subject><subject>Dietary Proteins - metabolism</subject><subject>Digestion</subject><subject>lysozyme</subject><subject>Muramidase - metabolism</subject><subject>Phosphorus</subject><subject>Phosphorus Compounds</subject><subject>phosphorus oxychloride</subject><subject>Phosphorylation</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLxDAURoMoOj5WroWudCHVm2Ty6E4dfIHoiAruQpqkTMdOMyYtTP31VmYYXAiu7uKc-13uh9AhhjMMBJ9PCwCMuYZhtoEGmBFIGcZyEw2gx6lkHO-g3RinACCZgG20zSWjkuMBuhhPfJxPfOgq3ZS-TnyRGB1dWSe6tknVRf_VzVySd8l8ZbYx8YvOTCofSuv20Vahq-gOVnMPvd1cv47u0oen2_vR5UOqqWRNKmROpCQ6pzwDZgSwzIBhhEmeU2sdWMqsY87mlmYF4Vpr0Hm_IfBQCGboHjpe5s6D_2xdbNSsjMZVla6db6OS_feCU_KviCmTmJCsF0-Xogk-xuAKNQ_lTIdOYVA_xapfxfb20Sq2zWfOrt1Vkz1Pl7yMjVussQ4figsqmHodv6jRzfvV86McK-j9k6WvTVRT34a6b-_Py99xYI6p</recordid><startdate>198303</startdate><enddate>198303</enddate><creator>Matheis, Guenter</creator><creator>Penner, Michael H</creator><creator>Feeney, Robert E</creator><creator>Whitaker, John R</creator><general>American Chemical Society</general><scope>BSCLL</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>C1K</scope><scope>7X8</scope></search><sort><creationdate>198303</creationdate><title>Phosphorylation of casein and lysozyme by phosphorus oxychloride</title><author>Matheis, Guenter ; Penner, Michael H ; Feeney, Robert E ; Whitaker, John R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a385t-78b2882ab36905c7059c0c52586b3dde0d35de5edbd39f26aaa0ab882714775c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>casein</topic><topic>Caseins - metabolism</topic><topic>Dietary Proteins - metabolism</topic><topic>Digestion</topic><topic>lysozyme</topic><topic>Muramidase - metabolism</topic><topic>Phosphorus</topic><topic>Phosphorus Compounds</topic><topic>phosphorus oxychloride</topic><topic>Phosphorylation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Matheis, Guenter</creatorcontrib><creatorcontrib>Penner, Michael H</creatorcontrib><creatorcontrib>Feeney, Robert E</creatorcontrib><creatorcontrib>Whitaker, John R</creatorcontrib><collection>Istex</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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Matheis, Guenter</au><au>Penner, Michael H</au><au>Feeney, Robert E</au><au>Whitaker, John R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of casein and lysozyme by phosphorus oxychloride</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1983-03</date><risdate>1983</risdate><volume>31</volume><issue>2</issue><spage>379</spage><epage>387</epage><pages>379-387</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><abstract>Casein and lysozyme were phosphorylated by phosphorus oxychloride at pH 6-8 and 3-20 degree C. Up to 7.4 and 6.2 mol of phosphate/mol of protein were covalently attached to casein and lysozyme, respectively. super(31)P NMR spectral data and pH stability studies of the phosphate residues indicated that in phosphorylated casein, the phosphate was exclusively bound to hydroxyl oxygen as monophosphate and diphosphate. The phosphate linkages were stable at pH 2.0-8.5. In contrast, the majority of the phosphate in phosphorylated lysozyme appeared to be bound to nitrogen. In addition to mono- and diphosphate, triphosphate bonds were present. Gel electrophoresis in the presence of sodium dodecyl sulfate and urea indicated that protein cross-linking occurred during phosphorylation.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>6853861</pmid><doi>10.1021/jf00116a049</doi><tpages>9</tpages></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 1983-03, Vol.31 (2), p.379-387 |
| issn | 0021-8561 1520-5118 |
| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | casein Caseins - metabolism Dietary Proteins - metabolism Digestion lysozyme Muramidase - metabolism Phosphorus Phosphorus Compounds phosphorus oxychloride Phosphorylation |
| title | Phosphorylation of casein and lysozyme by phosphorus oxychloride |
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