The relationship between reversibility of fibril formation and subunit composition of rat skin collagen
1. Salt-soluble rat skin collagen was precipitated from solution at neutral pH and 37 degrees . On cooling, a portion of the collagen returned into solution. The fractions were separated, the supernatant was concentrated and the precipitate was redissolved in dilute acetic acid. 2. Solutions of supe...
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| Veröffentlicht in: | Biochemical journal 1969-06, Vol.113 (2), p.419-422 |
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| creator | Bannister, D W |
| description | 1. Salt-soluble rat skin collagen was precipitated from solution at neutral pH and 37 degrees . On cooling, a portion of the collagen returned into solution. The fractions were separated, the supernatant was concentrated and the precipitate was redissolved in dilute acetic acid. 2. Solutions of supernatant and precipitate were subjected to the same fractionation procedure, giving four fractions. 3. Each fraction was examined by starch-gel electrophoresis and a relationship between subunit composition and the fractionation procedure was noted. The collagen that redissolved on cooling contained less of the more highly cross-linked components than did either the fraction remaining in the precipitate or the starting material. |
| doi_str_mv | 10.1042/bj1130419 |
| format | Article |
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Salt-soluble rat skin collagen was precipitated from solution at neutral pH and 37 degrees . On cooling, a portion of the collagen returned into solution. The fractions were separated, the supernatant was concentrated and the precipitate was redissolved in dilute acetic acid. 2. Solutions of supernatant and precipitate were subjected to the same fractionation procedure, giving four fractions. 3. Each fraction was examined by starch-gel electrophoresis and a relationship between subunit composition and the fractionation procedure was noted. 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Salt-soluble rat skin collagen was precipitated from solution at neutral pH and 37 degrees . On cooling, a portion of the collagen returned into solution. The fractions were separated, the supernatant was concentrated and the precipitate was redissolved in dilute acetic acid. 2. Solutions of supernatant and precipitate were subjected to the same fractionation procedure, giving four fractions. 3. Each fraction was examined by starch-gel electrophoresis and a relationship between subunit composition and the fractionation procedure was noted. The collagen that redissolved on cooling contained less of the more highly cross-linked components than did either the fraction remaining in the precipitate or the starting material.</description><subject>Animals</subject><subject>Chemical Precipitation</subject><subject>Collagen - analysis</subject><subject>Electrophoresis</subject><subject>Male</subject><subject>Rats</subject><subject>Skin - analysis</subject><subject>Solubility</subject><issn>0264-6021</issn><issn>0306-3283</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1969</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkUFv1DAQhS0EKtvCgR-A5BMSh8CM43XsCxKqgCJV4lLOlu1Mdl0Se7GTVv33hHa1gtNIbz69mafH2BuEDwhSfPS3iC1INM_YBmUHje6Efs42IJRsFAh8yc5rvQVACRLO2NlWg24FbtjuZk-80OjmmFPdxwP3NN8TpVW8o1Kjj2OcH3ge-BB9iSMfcpkeae5Sz-vilxRnHvJ0yDU-6itb3Mzrr5hWfRzdjtIr9mJwY6XXx3nBfn79cnN51Vz_-Pb98vN1E9oO5qYD03e6VbB1rWg7o4ymraZAwjuPpLcSpSf04E1HyoReBZQOSSmgoPquvWCfnnwPi5-oD5Tm4kZ7KHFy5cFmF-3_mxT3dpfvLKKWSprV4N3RoOTfC9XZTrEGWlMkyku1WgoJxogVfP8EhpJrLTScjiDYv63YUysr-_bfr07ksYb2D1fUipA</recordid><startdate>19690601</startdate><enddate>19690601</enddate><creator>Bannister, D W</creator><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><scope>5PM</scope></search><sort><creationdate>19690601</creationdate><title>The relationship between reversibility of fibril formation and subunit composition of rat skin collagen</title><author>Bannister, D W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c370t-709d783605a32379698e58ece2bab1e85414be1b0b97e69cd6c14a1e660ec6d73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1969</creationdate><topic>Animals</topic><topic>Chemical Precipitation</topic><topic>Collagen - analysis</topic><topic>Electrophoresis</topic><topic>Male</topic><topic>Rats</topic><topic>Skin - analysis</topic><topic>Solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bannister, D W</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bannister, D W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The relationship between reversibility of fibril formation and subunit composition of rat skin collagen</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1969-06-01</date><risdate>1969</risdate><volume>113</volume><issue>2</issue><spage>419</spage><epage>422</epage><pages>419-422</pages><issn>0264-6021</issn><issn>0306-3283</issn><eissn>1470-8728</eissn><abstract>1. Salt-soluble rat skin collagen was precipitated from solution at neutral pH and 37 degrees . On cooling, a portion of the collagen returned into solution. The fractions were separated, the supernatant was concentrated and the precipitate was redissolved in dilute acetic acid. 2. Solutions of supernatant and precipitate were subjected to the same fractionation procedure, giving four fractions. 3. Each fraction was examined by starch-gel electrophoresis and a relationship between subunit composition and the fractionation procedure was noted. The collagen that redissolved on cooling contained less of the more highly cross-linked components than did either the fraction remaining in the precipitate or the starting material.</abstract><cop>England</cop><pmid>5808321</pmid><doi>10.1042/bj1130419</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemical journal, 1969-06, Vol.113 (2), p.419-422 |
| issn | 0264-6021 0306-3283 1470-8728 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Animals Chemical Precipitation Collagen - analysis Electrophoresis Male Rats Skin - analysis Solubility |
| title | The relationship between reversibility of fibril formation and subunit composition of rat skin collagen |
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