Molecular weights of blood plasma fractions photooxidized in the presence of sensitizers
Sensitized photooxidation of human blood plasma fractions, in contrast to high frequency electromagnetic irradiation of them, did not cause molecular splitting. On the contrary, an increase of the molecular weight was observed. This increase was, however, due only to the aggregation of a part of the...
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Veröffentlicht in: | Biochimica et biophysica acta 1961-05, Vol.49 (3), p.495-501 |
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creator | Vodrážka, Zdeněk Mach, Otakar |
description | Sensitized photooxidation of human blood plasma fractions, in contrast to high frequency electromagnetic irradiation of them, did not cause molecular splitting. On the contrary, an increase of the molecular weight was observed. This increase was, however, due only to the aggregation of a part of the molecules and its degree depend markedly on certain reaction conditions, such as temperature and protein concentration.
By conducting the reaction at low temperature and low protein concentration and by reducing the reaction time, it was possible, at any rate when human serum albumin, γ-globulin and fibrinogen were used, to obtain photooxidized proteins of unchanged molecular weight. The fractions aggregated were separated by precipitation with ammonium sulphate. In order to maintain the molecular weight unchanged, sensitization by eosin seemed to be preferable to sensitization by methylene blue. The influence of photooxidation on sensitizer-protein interactions is discussed. |
doi_str_mv | 10.1016/0006-3002(61)90246-3 |
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By conducting the reaction at low temperature and low protein concentration and by reducing the reaction time, it was possible, at any rate when human serum albumin, γ-globulin and fibrinogen were used, to obtain photooxidized proteins of unchanged molecular weight. The fractions aggregated were separated by precipitation with ammonium sulphate. In order to maintain the molecular weight unchanged, sensitization by eosin seemed to be preferable to sensitization by methylene blue. The influence of photooxidation on sensitizer-protein interactions is discussed.</description><identifier>ISSN: 0006-3002</identifier><identifier>EISSN: 1878-2434</identifier><identifier>DOI: 10.1016/0006-3002(61)90246-3</identifier><identifier>PMID: 13781768</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Blood Proteins - chemistry ; Learning ; Molecular Weight ; Old Medline ; Plasma ; Proteins</subject><ispartof>Biochimica et biophysica acta, 1961-05, Vol.49 (3), p.495-501</ispartof><rights>1961</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c360t-db494a251bf0f540d2d9a9e9d4edf043b293ae27d62b67efcb6b36a903d40d263</citedby><cites>FETCH-LOGICAL-c360t-db494a251bf0f540d2d9a9e9d4edf043b293ae27d62b67efcb6b36a903d40d263</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/13781768$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vodrážka, Zdeněk</creatorcontrib><creatorcontrib>Mach, Otakar</creatorcontrib><title>Molecular weights of blood plasma fractions photooxidized in the presence of sensitizers</title><title>Biochimica et biophysica acta</title><addtitle>Biochim Biophys Acta</addtitle><description>Sensitized photooxidation of human blood plasma fractions, in contrast to high frequency electromagnetic irradiation of them, did not cause molecular splitting. On the contrary, an increase of the molecular weight was observed. This increase was, however, due only to the aggregation of a part of the molecules and its degree depend markedly on certain reaction conditions, such as temperature and protein concentration.
By conducting the reaction at low temperature and low protein concentration and by reducing the reaction time, it was possible, at any rate when human serum albumin, γ-globulin and fibrinogen were used, to obtain photooxidized proteins of unchanged molecular weight. The fractions aggregated were separated by precipitation with ammonium sulphate. In order to maintain the molecular weight unchanged, sensitization by eosin seemed to be preferable to sensitization by methylene blue. The influence of photooxidation on sensitizer-protein interactions is discussed.</description><subject>Blood Proteins - chemistry</subject><subject>Learning</subject><subject>Molecular Weight</subject><subject>Old Medline</subject><subject>Plasma</subject><subject>Proteins</subject><issn>0006-3002</issn><issn>1878-2434</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1961</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LxDAQhoMo7rr6D0RyEj1U89W0vQiy-AWKFwVvIU2mbqTd1KT169fbuovePGXCPO8M8yC0T8kJJVSeEkJkwglhR5IeF4SJ4beBpjTP8oQJLjbR9BeZoJ0YX4Yi5aTYRhPKs5xmMp-ipztfg-lrHfA7uOdFF7GvcFl7b3Fb69hoXAVtOueXEbcL33n_4az7AovdEncLwG2ACEsDY24oouuGboi7aKvSdYS99TtDj5cXD_Pr5Pb-6mZ-fpsYLkmX2FIUQrOUlhWpUkEss4UuoLACbEUEL1nBNbDMSlbKDCpTypJLXRBuR1jyGTpczW2Df-0hdqpx0UBd6yX4Pqqc5YIRkQ6gWIEm-BgDVKoNrtHhU1GiRqNq1KVGXUpS9WNU8SF2sJ7flw3Yv9Ba4QCcrQAYrnxzEFQ0bhRiXQDTKevd_xu-ASi-hn4</recordid><startdate>19610527</startdate><enddate>19610527</enddate><creator>Vodrážka, Zdeněk</creator><creator>Mach, Otakar</creator><general>Elsevier B.V</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>19610527</creationdate><title>Molecular weights of blood plasma fractions photooxidized in the presence of sensitizers</title><author>Vodrážka, Zdeněk ; Mach, Otakar</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c360t-db494a251bf0f540d2d9a9e9d4edf043b293ae27d62b67efcb6b36a903d40d263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1961</creationdate><topic>Blood Proteins - chemistry</topic><topic>Learning</topic><topic>Molecular Weight</topic><topic>Old Medline</topic><topic>Plasma</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vodrážka, Zdeněk</creatorcontrib><creatorcontrib>Mach, Otakar</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>Biochimica et biophysica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vodrážka, Zdeněk</au><au>Mach, Otakar</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular weights of blood plasma fractions photooxidized in the presence of sensitizers</atitle><jtitle>Biochimica et biophysica acta</jtitle><addtitle>Biochim Biophys Acta</addtitle><date>1961-05-27</date><risdate>1961</risdate><volume>49</volume><issue>3</issue><spage>495</spage><epage>501</epage><pages>495-501</pages><issn>0006-3002</issn><eissn>1878-2434</eissn><abstract>Sensitized photooxidation of human blood plasma fractions, in contrast to high frequency electromagnetic irradiation of them, did not cause molecular splitting. On the contrary, an increase of the molecular weight was observed. This increase was, however, due only to the aggregation of a part of the molecules and its degree depend markedly on certain reaction conditions, such as temperature and protein concentration.
By conducting the reaction at low temperature and low protein concentration and by reducing the reaction time, it was possible, at any rate when human serum albumin, γ-globulin and fibrinogen were used, to obtain photooxidized proteins of unchanged molecular weight. The fractions aggregated were separated by precipitation with ammonium sulphate. In order to maintain the molecular weight unchanged, sensitization by eosin seemed to be preferable to sensitization by methylene blue. The influence of photooxidation on sensitizer-protein interactions is discussed.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>13781768</pmid><doi>10.1016/0006-3002(61)90246-3</doi><tpages>7</tpages></addata></record> |
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subjects | Blood Proteins - chemistry Learning Molecular Weight Old Medline Plasma Proteins |
title | Molecular weights of blood plasma fractions photooxidized in the presence of sensitizers |
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