Identification of the κ-Casein Among the Components of Whole Goat Casein
Goat κ-casein in the reduced state, probably the natural state, has a mobility on acrylamide gel electrophoresis at pH 9, very close to that of the β-caseins. The goat κ-casein was identified by clotting with rennin, by specific changes in the electrophoretic pattern after rennin action, and by nonp...
Gespeichert in:
| Veröffentlicht in: | Journal of dairy science 1966-07, Vol.49 (7), p.788-791 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 791 |
|---|---|
| container_issue | 7 |
| container_start_page | 788 |
| container_title | Journal of dairy science |
| container_volume | 49 |
| creator | Zittle, C.A. Custer, J.H. |
| description | Goat κ-casein in the reduced state, probably the natural state, has a mobility on acrylamide gel electrophoresis at pH 9, very close to that of the β-caseins. The goat κ-casein was identified by clotting with rennin, by specific changes in the electrophoretic pattern after rennin action, and by nonprecipitation with calcium ions. It stabilized goat αs-casein so that αs-casein was not precipitated with calcium ions. Polyacrylamide gel electrophoresis of goat κ-casein in some cases gave a single band (together with identifiable contaminants), and, in other cases, gave a multiplicity of slower-moving bands. In all cases only a single major band was observed when the κ-casein was reduced with mercaptoethanol. Components with the mobilities of para-κ-casein were present in considerable amounts in some preparations of κ-casein. |
| doi_str_mv | 10.3168/jds.S0022-0302(66)87946-8 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_84318644</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0022030266879468</els_id><sourcerecordid>1839847983</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3668-dc840ad6dfd60b2179cab12d4dac351bafa4765dacf866ff4202f1f84a7609fd3</originalsourceid><addsrcrecordid>eNqNkMtKw0AUQAdRaq1-ghARRBep88pksixBa6HgQsXlMJ2HndJkaiYR_DU_wm9y2hQXrlxd7r3nPjgAXCA4Jojx25UO4ycIMU4hgfiasRueF5Sl_AAMUYazlKCCH4LhL3IMTkJYxRRhmA3AgEGY55wPwWymTd0665Rsna8Tb5N2aZLvr7SUwbg6mVS-ftvVSl9tfB3psKVel35tkqmXbdKTp-DIynUwZ_s4Ai_3d8_lQzp_nM7KyTxVhDGeasUplJppqxlcYJQXSi4Q1lRLRTK0kFbSnGUxs5wxaymG2CLLqcwZLKwmI3DV7900_r0zoRWVC8qs17I2vguCU4I4ozSCl3_Ale-aOv4mECcFp3nBSaSKnlKND6ExVmwaV8nmUyAotrJFlC12ssXWpGBM7GQLHmfP9xe6RWX07-TebuyXfd9EHx_ONCIoZ2pltGuMaoX27h9XfgDHYZGB</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1839847983</pqid></control><display><type>article</type><title>Identification of the κ-Casein Among the Components of Whole Goat Casein</title><source>Elsevier ScienceDirect Journals Complete - AutoHoldings</source><source>MEDLINE</source><source>Periodicals Index Online</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>Zittle, C.A. ; Custer, J.H.</creator><creatorcontrib>Zittle, C.A. ; Custer, J.H.</creatorcontrib><description>Goat κ-casein in the reduced state, probably the natural state, has a mobility on acrylamide gel electrophoresis at pH 9, very close to that of the β-caseins. The goat κ-casein was identified by clotting with rennin, by specific changes in the electrophoretic pattern after rennin action, and by nonprecipitation with calcium ions. It stabilized goat αs-casein so that αs-casein was not precipitated with calcium ions. Polyacrylamide gel electrophoresis of goat κ-casein in some cases gave a single band (together with identifiable contaminants), and, in other cases, gave a multiplicity of slower-moving bands. In all cases only a single major band was observed when the κ-casein was reduced with mercaptoethanol. Components with the mobilities of para-κ-casein were present in considerable amounts in some preparations of κ-casein.</description><identifier>ISSN: 0022-0302</identifier><identifier>EISSN: 1525-3198</identifier><identifier>DOI: 10.3168/jds.S0022-0302(66)87946-8</identifier><identifier>PMID: 6007788</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Caseins - analysis ; Electrophoresis ; Goats ; Milk - analysis ; Renin - pharmacology</subject><ispartof>Journal of dairy science, 1966-07, Vol.49 (7), p.788-791</ispartof><rights>1966 American Dairy Science Association</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3668-dc840ad6dfd60b2179cab12d4dac351bafa4765dacf866ff4202f1f84a7609fd3</citedby><cites>FETCH-LOGICAL-c3668-dc840ad6dfd60b2179cab12d4dac351bafa4765dacf866ff4202f1f84a7609fd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.3168/jds.S0022-0302(66)87946-8$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27868,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6007788$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zittle, C.A.</creatorcontrib><creatorcontrib>Custer, J.H.</creatorcontrib><title>Identification of the κ-Casein Among the Components of Whole Goat Casein</title><title>Journal of dairy science</title><addtitle>J Dairy Sci</addtitle><description>Goat κ-casein in the reduced state, probably the natural state, has a mobility on acrylamide gel electrophoresis at pH 9, very close to that of the β-caseins. The goat κ-casein was identified by clotting with rennin, by specific changes in the electrophoretic pattern after rennin action, and by nonprecipitation with calcium ions. It stabilized goat αs-casein so that αs-casein was not precipitated with calcium ions. Polyacrylamide gel electrophoresis of goat κ-casein in some cases gave a single band (together with identifiable contaminants), and, in other cases, gave a multiplicity of slower-moving bands. In all cases only a single major band was observed when the κ-casein was reduced with mercaptoethanol. Components with the mobilities of para-κ-casein were present in considerable amounts in some preparations of κ-casein.</description><subject>Animals</subject><subject>Caseins - analysis</subject><subject>Electrophoresis</subject><subject>Goats</subject><subject>Milk - analysis</subject><subject>Renin - pharmacology</subject><issn>0022-0302</issn><issn>1525-3198</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1966</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>K30</sourceid><recordid>eNqNkMtKw0AUQAdRaq1-ghARRBep88pksixBa6HgQsXlMJ2HndJkaiYR_DU_wm9y2hQXrlxd7r3nPjgAXCA4Jojx25UO4ycIMU4hgfiasRueF5Sl_AAMUYazlKCCH4LhL3IMTkJYxRRhmA3AgEGY55wPwWymTd0665Rsna8Tb5N2aZLvr7SUwbg6mVS-ftvVSl9tfB3psKVel35tkqmXbdKTp-DIynUwZ_s4Ai_3d8_lQzp_nM7KyTxVhDGeasUplJppqxlcYJQXSi4Q1lRLRTK0kFbSnGUxs5wxaymG2CLLqcwZLKwmI3DV7900_r0zoRWVC8qs17I2vguCU4I4ozSCl3_Ale-aOv4mECcFp3nBSaSKnlKND6ExVmwaV8nmUyAotrJFlC12ssXWpGBM7GQLHmfP9xe6RWX07-TebuyXfd9EHx_ONCIoZ2pltGuMaoX27h9XfgDHYZGB</recordid><startdate>196607</startdate><enddate>196607</enddate><creator>Zittle, C.A.</creator><creator>Custer, J.H.</creator><general>Elsevier Inc</general><general>American Dairy Science Association</general><scope>6I.</scope><scope>AAFTH</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>7WH</scope><scope>K30</scope><scope>PAAUG</scope><scope>PAWHS</scope><scope>PAWZZ</scope><scope>PAXOH</scope><scope>PBHAV</scope><scope>PBQSW</scope><scope>PBYQZ</scope><scope>PCIWU</scope><scope>PCMID</scope><scope>PCZJX</scope><scope>PDGRG</scope><scope>PDWWI</scope><scope>PETMR</scope><scope>PFVGT</scope><scope>PGXDX</scope><scope>PIHIL</scope><scope>PISVA</scope><scope>PJCTQ</scope><scope>PJTMS</scope><scope>PLCHJ</scope><scope>PMHAD</scope><scope>PNQDJ</scope><scope>POUND</scope><scope>PPLAD</scope><scope>PQAPC</scope><scope>PQCAN</scope><scope>PQCMW</scope><scope>PQEME</scope><scope>PQHKH</scope><scope>PQMID</scope><scope>PQNCT</scope><scope>PQNET</scope><scope>PQSCT</scope><scope>PQSET</scope><scope>PSVJG</scope><scope>PVMQY</scope><scope>PZGFC</scope><scope>7X8</scope></search><sort><creationdate>196607</creationdate><title>Identification of the κ-Casein Among the Components of Whole Goat Casein</title><author>Zittle, C.A. ; Custer, J.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3668-dc840ad6dfd60b2179cab12d4dac351bafa4765dacf866ff4202f1f84a7609fd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1966</creationdate><topic>Animals</topic><topic>Caseins - analysis</topic><topic>Electrophoresis</topic><topic>Goats</topic><topic>Milk - analysis</topic><topic>Renin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zittle, C.A.</creatorcontrib><creatorcontrib>Custer, J.H.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Periodicals Index Online Segment 50</collection><collection>Periodicals Index Online</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - West</collection><collection>Primary Sources Access (Plan D) - International</collection><collection>Primary Sources Access & Build (Plan A) - MEA</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - Midwest</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - Northeast</collection><collection>Primary Sources Access (Plan D) - Southeast</collection><collection>Primary Sources Access (Plan D) - North Central</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - Southeast</collection><collection>Primary Sources Access (Plan D) - South Central</collection><collection>Primary Sources Access & Build (Plan A) - UK / I</collection><collection>Primary Sources Access (Plan D) - Canada</collection><collection>Primary Sources Access (Plan D) - EMEALA</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - North Central</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - South Central</collection><collection>Primary Sources Access & Build (Plan A) - International</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - International</collection><collection>Primary Sources Access (Plan D) - West</collection><collection>Periodicals Index Online Segments 1-50</collection><collection>Primary Sources Access (Plan D) - APAC</collection><collection>Primary Sources Access (Plan D) - Midwest</collection><collection>Primary Sources Access (Plan D) - MEA</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - Canada</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - UK / I</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - EMEALA</collection><collection>Primary Sources Access & Build (Plan A) - APAC</collection><collection>Primary Sources Access & Build (Plan A) - Canada</collection><collection>Primary Sources Access & Build (Plan A) - West</collection><collection>Primary Sources Access & Build (Plan A) - EMEALA</collection><collection>Primary Sources Access (Plan D) - Northeast</collection><collection>Primary Sources Access & Build (Plan A) - Midwest</collection><collection>Primary Sources Access & Build (Plan A) - North Central</collection><collection>Primary Sources Access & Build (Plan A) - Northeast</collection><collection>Primary Sources Access & Build (Plan A) - South Central</collection><collection>Primary Sources Access & Build (Plan A) - Southeast</collection><collection>Primary Sources Access (Plan D) - UK / I</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - APAC</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - MEA</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of dairy science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zittle, C.A.</au><au>Custer, J.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of the κ-Casein Among the Components of Whole Goat Casein</atitle><jtitle>Journal of dairy science</jtitle><addtitle>J Dairy Sci</addtitle><date>1966-07</date><risdate>1966</risdate><volume>49</volume><issue>7</issue><spage>788</spage><epage>791</epage><pages>788-791</pages><issn>0022-0302</issn><eissn>1525-3198</eissn><abstract>Goat κ-casein in the reduced state, probably the natural state, has a mobility on acrylamide gel electrophoresis at pH 9, very close to that of the β-caseins. The goat κ-casein was identified by clotting with rennin, by specific changes in the electrophoretic pattern after rennin action, and by nonprecipitation with calcium ions. It stabilized goat αs-casein so that αs-casein was not precipitated with calcium ions. Polyacrylamide gel electrophoresis of goat κ-casein in some cases gave a single band (together with identifiable contaminants), and, in other cases, gave a multiplicity of slower-moving bands. In all cases only a single major band was observed when the κ-casein was reduced with mercaptoethanol. Components with the mobilities of para-κ-casein were present in considerable amounts in some preparations of κ-casein.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6007788</pmid><doi>10.3168/jds.S0022-0302(66)87946-8</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-0302 |
| ispartof | Journal of dairy science, 1966-07, Vol.49 (7), p.788-791 |
| issn | 0022-0302 1525-3198 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_84318644 |
| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE; Periodicals Index Online; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Caseins - analysis Electrophoresis Goats Milk - analysis Renin - pharmacology |
| title | Identification of the κ-Casein Among the Components of Whole Goat Casein |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-09T06%3A17%3A06IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20of%20the%20%CE%BA-Casein%20Among%20the%20Components%20of%20Whole%20Goat%20Casein&rft.jtitle=Journal%20of%20dairy%20science&rft.au=Zittle,%20C.A.&rft.date=1966-07&rft.volume=49&rft.issue=7&rft.spage=788&rft.epage=791&rft.pages=788-791&rft.issn=0022-0302&rft.eissn=1525-3198&rft_id=info:doi/10.3168/jds.S0022-0302(66)87946-8&rft_dat=%3Cproquest_cross%3E1839847983%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1839847983&rft_id=info:pmid/6007788&rft_els_id=S0022030266879468&rfr_iscdi=true |