Light-scattering study of effect of electrolytes on α- and β-casein solutions
Solutions of α- and β-casein are aggregated by electrolytes. This contrasts with the behavior of native ovalbumin, serum albumin, and lactoglobulin, but resembles that of the denatured forms of these proteins (the latter two after addition of ethanol). It is concluded that the caseins have the prope...
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Veröffentlicht in: | Archives of biochemistry and biophysics 1954-07, Vol.51 (1), p.79-87 |
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creator | Halwer, Murray |
description | Solutions of α- and β-casein are aggregated by electrolytes. This contrasts with the behavior of native ovalbumin, serum albumin, and lactoglobulin, but resembles that of the denatured forms of these proteins (the latter two after addition of ethanol). It is concluded that the caseins have the properties of denatured proteins. Determination of their molecular weights is complicated by the aggregation effect, and values in which confidence can be felt probably do not now exist. |
doi_str_mv | 10.1016/0003-9861(54)90455-5 |
format | Article |
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This contrasts with the behavior of native ovalbumin, serum albumin, and lactoglobulin, but resembles that of the denatured forms of these proteins (the latter two after addition of ethanol). It is concluded that the caseins have the properties of denatured proteins. Determination of their molecular weights is complicated by the aggregation effect, and values in which confidence can be felt probably do not now exist.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(54)90455-5</identifier><identifier>PMID: 13181462</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Caseins ; Electrolytes - pharmacology ; Old Medline ; Solutions</subject><ispartof>Archives of biochemistry and biophysics, 1954-07, Vol.51 (1), p.79-87</ispartof><rights>1954</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c275t-db6bbf25483c70fffd2c6ee6b7c3bd06c9d83df8fe97f72753aed5c226e917103</citedby><cites>FETCH-LOGICAL-c275t-db6bbf25483c70fffd2c6ee6b7c3bd06c9d83df8fe97f72753aed5c226e917103</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(54)90455-5$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/13181462$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Halwer, Murray</creatorcontrib><title>Light-scattering study of effect of electrolytes on α- and β-casein solutions</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Solutions of α- and β-casein are aggregated by electrolytes. This contrasts with the behavior of native ovalbumin, serum albumin, and lactoglobulin, but resembles that of the denatured forms of these proteins (the latter two after addition of ethanol). It is concluded that the caseins have the properties of denatured proteins. Determination of their molecular weights is complicated by the aggregation effect, and values in which confidence can be felt probably do not now exist.</description><subject>Caseins</subject><subject>Electrolytes - pharmacology</subject><subject>Old Medline</subject><subject>Solutions</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1954</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtOwzAQRS0EouXxBwhlhWBhsBPbSTZIqOIlVeoG1lZij4tRGhfbQepnwYf0m0jaCnas5i7OndEchM4ouaaEihtCSIbLQtBLzq5KwjjHfA-NKSkFJlnB9tH4FxmhoxDeCaGUifQQjWhGiyGO0Wxq528RB1XFCN628yTETq8SZxIwBlTcpKYP3jWrCCFxbbL-wknV6mT9jVUVwLZJcE0XrWvDCTowVRPgdDeP0evD_cvkCU9nj8-TuylWac4j1rWoa5NyVmQqJ8YYnSoBIOpcZbUmQpW6yLQpDJS5yftKVoHmKk0FlDSnJDtGF9u9S-8-OghRLmxQ0DRVC64LMhdp_zwTPci2oPIuBA9GLr1dVH4lKZGDSDlYkoMlyZnciJS8r53v9nf1AvRfaWeuB263APRfflrwMigLrQJtfW9Lamf_v_ADx-SENw</recordid><startdate>195407</startdate><enddate>195407</enddate><creator>Halwer, Murray</creator><general>Elsevier Inc</general><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>7X8</scope></search><sort><creationdate>195407</creationdate><title>Light-scattering study of effect of electrolytes on α- and β-casein solutions</title><author>Halwer, Murray</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c275t-db6bbf25483c70fffd2c6ee6b7c3bd06c9d83df8fe97f72753aed5c226e917103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1954</creationdate><topic>Caseins</topic><topic>Electrolytes - pharmacology</topic><topic>Old Medline</topic><topic>Solutions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Halwer, Murray</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</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>Halwer, Murray</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Light-scattering study of effect of electrolytes on α- and β-casein solutions</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1954-07</date><risdate>1954</risdate><volume>51</volume><issue>1</issue><spage>79</spage><epage>87</epage><pages>79-87</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Solutions of α- and β-casein are aggregated by electrolytes. This contrasts with the behavior of native ovalbumin, serum albumin, and lactoglobulin, but resembles that of the denatured forms of these proteins (the latter two after addition of ethanol). It is concluded that the caseins have the properties of denatured proteins. Determination of their molecular weights is complicated by the aggregation effect, and values in which confidence can be felt probably do not now exist.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>13181462</pmid><doi>10.1016/0003-9861(54)90455-5</doi><tpages>9</tpages></addata></record> |
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ispartof | Archives of biochemistry and biophysics, 1954-07, Vol.51 (1), p.79-87 |
issn | 0003-9861 1096-0384 |
language | eng |
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source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
subjects | Caseins Electrolytes - pharmacology Old Medline Solutions |
title | Light-scattering study of effect of electrolytes on α- and β-casein solutions |
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