Molecular Weight of Ovalbumin and of Bovine Serum Albumin in Urea Solution
SINCE 1902, when Ramsden 1 described the effects of urea on “proteids”, there has been much speculation regarding the molecular weights of proteins in urea solution. Some workers have claimed that aggregation does not take place in the urea denaturation of ovalbumin and bovine serum albumin. In spit...
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Veröffentlicht in: | Nature (London) 1955-10, Vol.176 (4485), p.738-738 |
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creator | McKENZIE, H. A SMITH, M. B WAKE, R. G |
description | SINCE 1902, when Ramsden
1
described the effects of urea on “proteids”, there has been much speculation regarding the molecular weights of proteins in urea solution. Some workers have claimed that aggregation does not take place in the urea denaturation of ovalbumin and bovine serum albumin. In spite of this, it is well known that their urea solutions frequently form gels when the protein concentration is high. Recently, Kauzmann
et al.
2,3
have studied the viscosity changes accompanying the urea denaturation of these proteins and the gelling time for ovalbumin. Under certain conditions an aggregation dependent upon concentration occurred, and this was interpreted in terms of hydrogen bonding and inter-molecular disulphide bonds (the latter through the —SS— and —SH exchange reaction of Huggins, Tapley and Jensen
4
). |
doi_str_mv | 10.1038/176738a0 |
format | Article |
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1
described the effects of urea on “proteids”, there has been much speculation regarding the molecular weights of proteins in urea solution. Some workers have claimed that aggregation does not take place in the urea denaturation of ovalbumin and bovine serum albumin. In spite of this, it is well known that their urea solutions frequently form gels when the protein concentration is high. Recently, Kauzmann
et al.
2,3
have studied the viscosity changes accompanying the urea denaturation of these proteins and the gelling time for ovalbumin. Under certain conditions an aggregation dependent upon concentration occurred, and this was interpreted in terms of hydrogen bonding and inter-molecular disulphide bonds (the latter through the —SS— and —SH exchange reaction of Huggins, Tapley and Jensen
4
).</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/176738a0</identifier><identifier>PMID: 13265819</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Albumins ; Humanities and Social Sciences ; letter ; Molecular Weight ; multidisciplinary ; Old Medline ; Ovalbumin ; Science ; Science (multidisciplinary) ; Serum Albumin ; Serum Albumin, Bovine ; Solutions ; Urea</subject><ispartof>Nature (London), 1955-10, Vol.176 (4485), p.738-738</ispartof><rights>Springer Nature Limited 1955</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c370t-5aad51370c6f4a3c046914f6ea3b6c4912b29d90c951e2c2b734c58bf94bc1f73</citedby><cites>FETCH-LOGICAL-c370t-5aad51370c6f4a3c046914f6ea3b6c4912b29d90c951e2c2b734c58bf94bc1f73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/176738a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/176738a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,2725,27922,27923,41486,42555,51317</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/13265819$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McKENZIE, H. A</creatorcontrib><creatorcontrib>SMITH, M. B</creatorcontrib><creatorcontrib>WAKE, R. G</creatorcontrib><title>Molecular Weight of Ovalbumin and of Bovine Serum Albumin in Urea Solution</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>SINCE 1902, when Ramsden
1
described the effects of urea on “proteids”, there has been much speculation regarding the molecular weights of proteins in urea solution. Some workers have claimed that aggregation does not take place in the urea denaturation of ovalbumin and bovine serum albumin. In spite of this, it is well known that their urea solutions frequently form gels when the protein concentration is high. Recently, Kauzmann
et al.
2,3
have studied the viscosity changes accompanying the urea denaturation of these proteins and the gelling time for ovalbumin. Under certain conditions an aggregation dependent upon concentration occurred, and this was interpreted in terms of hydrogen bonding and inter-molecular disulphide bonds (the latter through the —SS— and —SH exchange reaction of Huggins, Tapley and Jensen
4
).</description><subject>Albumins</subject><subject>Humanities and Social Sciences</subject><subject>letter</subject><subject>Molecular Weight</subject><subject>multidisciplinary</subject><subject>Old Medline</subject><subject>Ovalbumin</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Serum Albumin</subject><subject>Serum Albumin, Bovine</subject><subject>Solutions</subject><subject>Urea</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1955</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LAzEQhoMotlbBXyB7Ej2sJpvvoxY_qfRQi8clm2brlt2kJpuC_94t3dKbMDDDzMMD8wJwieAdgljcI844FgoegSEinKWECX4MhhBmIoUCswE4C2EFIaSIk1MwQDhjVCA5BO8frjY61sonX6ZafreJK5PpRtVFbCqbKLvYLh7dprImmRkfm-Shv3U190YlM1fHtnL2HJyUqg7mou8jMH9--hy_ppPpy9v4YZJqzGGbUqUWFHWjZiVRWEPCJCIlMwoXTBOJsiKTCwm1pMhkOis4JpqKopSk0KjkeASud961dz_RhDZvqqBNXStrXAy5QFRQLGQH3uxA7V0I3pT52leN8r85gvk2t3yfW4de9c5YNGZxAPugOuB2B4TuZJfG5ysXve3-_EdmVRu9Ocj2wB-rbn37</recordid><startdate>19551015</startdate><enddate>19551015</enddate><creator>McKENZIE, H. A</creator><creator>SMITH, M. B</creator><creator>WAKE, R. G</creator><general>Nature Publishing Group UK</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>19551015</creationdate><title>Molecular Weight of Ovalbumin and of Bovine Serum Albumin in Urea Solution</title><author>McKENZIE, H. A ; SMITH, M. B ; WAKE, R. G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c370t-5aad51370c6f4a3c046914f6ea3b6c4912b29d90c951e2c2b734c58bf94bc1f73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1955</creationdate><topic>Albumins</topic><topic>Humanities and Social Sciences</topic><topic>letter</topic><topic>Molecular Weight</topic><topic>multidisciplinary</topic><topic>Old Medline</topic><topic>Ovalbumin</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Serum Albumin</topic><topic>Serum Albumin, Bovine</topic><topic>Solutions</topic><topic>Urea</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McKENZIE, H. A</creatorcontrib><creatorcontrib>SMITH, M. B</creatorcontrib><creatorcontrib>WAKE, R. G</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>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McKENZIE, H. A</au><au>SMITH, M. B</au><au>WAKE, R. G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Weight of Ovalbumin and of Bovine Serum Albumin in Urea Solution</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1955-10-15</date><risdate>1955</risdate><volume>176</volume><issue>4485</issue><spage>738</spage><epage>738</epage><pages>738-738</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><abstract>SINCE 1902, when Ramsden
1
described the effects of urea on “proteids”, there has been much speculation regarding the molecular weights of proteins in urea solution. Some workers have claimed that aggregation does not take place in the urea denaturation of ovalbumin and bovine serum albumin. In spite of this, it is well known that their urea solutions frequently form gels when the protein concentration is high. Recently, Kauzmann
et al.
2,3
have studied the viscosity changes accompanying the urea denaturation of these proteins and the gelling time for ovalbumin. Under certain conditions an aggregation dependent upon concentration occurred, and this was interpreted in terms of hydrogen bonding and inter-molecular disulphide bonds (the latter through the —SS— and —SH exchange reaction of Huggins, Tapley and Jensen
4
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subjects | Albumins Humanities and Social Sciences letter Molecular Weight multidisciplinary Old Medline Ovalbumin Science Science (multidisciplinary) Serum Albumin Serum Albumin, Bovine Solutions Urea |
title | Molecular Weight of Ovalbumin and of Bovine Serum Albumin in Urea Solution |
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