Purification and Partial Characterization of a Basic Protein from Pig Brain
A basic protein has been isolated from pig brain. The purification procedure consisted of repeated extractions with chloroform-methanol (2:1 v/v), 10% sodium chloride, and dilute hydrochloric acid. The pH 2.4 to 2.6 fraction obtained from the repeated acid extraction was further purified by pH and (...
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| Veröffentlicht in: | The Journal of biological chemistry 1967-11, Vol.242 (21), p.4933-4938 |
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| container_end_page | 4938 |
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| container_title | The Journal of biological chemistry |
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| creator | Tomasi, L G Kornguth, S E |
| description | A basic protein has been isolated from pig brain. The purification procedure consisted of repeated extractions with chloroform-methanol
(2:1 v/v), 10% sodium chloride, and dilute hydrochloric acid. The pH 2.4 to 2.6 fraction obtained from the repeated acid extraction
was further purified by pH and (NH 4 ) 2 SO 4 fractionation, Sephadex G-100 gel filtration, and chromatography on Amberlite IRC-50 with a gradient (5 to 20%) of guanidinium
chloride. All of the fractions obtained by this purification procedure have been examined by starch gel electrophoresis.
The homogeneity of the pig brain basic protein has been established by ultracentrifugation, starch gel electrophoresis, polyacrylamide
gel electrophoresis, and end group analysis. Amino acid analysis performed on a complete acid hydrolysate of the protein indicated
that the ratio of basic to acidic amino acids is greater than 1.5. An absence of cysteine and the presence of a high glycine
and proline content have also been observed. |
| doi_str_mv | 10.1016/S0021-9258(18)99459-7 |
| format | Article |
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(2:1 v/v), 10% sodium chloride, and dilute hydrochloric acid. The pH 2.4 to 2.6 fraction obtained from the repeated acid extraction
was further purified by pH and (NH 4 ) 2 SO 4 fractionation, Sephadex G-100 gel filtration, and chromatography on Amberlite IRC-50 with a gradient (5 to 20%) of guanidinium
chloride. All of the fractions obtained by this purification procedure have been examined by starch gel electrophoresis.
The homogeneity of the pig brain basic protein has been established by ultracentrifugation, starch gel electrophoresis, polyacrylamide
gel electrophoresis, and end group analysis. Amino acid analysis performed on a complete acid hydrolysate of the protein indicated
that the ratio of basic to acidic amino acids is greater than 1.5. An absence of cysteine and the presence of a high glycine
and proline content have also been observed.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)99459-7</identifier><identifier>PMID: 6058938</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Acrylic Resins ; Amino Acids - analysis ; Animals ; Brain Chemistry ; Chromatography, Gel ; Chromatography, Ion Exchange ; Electrophoresis ; Hydrogen-Ion Concentration ; Nerve Tissue Proteins - analysis ; Swine ; Ultracentrifugation</subject><ispartof>The Journal of biological chemistry, 1967-11, Vol.242 (21), p.4933-4938</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c379t-4ae246443f8c71413fb0eadd9a48e99f6cd7b32c7d4c1cc1d543992f2cc0ba1f3</citedby><cites>FETCH-LOGICAL-c379t-4ae246443f8c71413fb0eadd9a48e99f6cd7b32c7d4c1cc1d543992f2cc0ba1f3</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/6058938$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tomasi, L G</creatorcontrib><creatorcontrib>Kornguth, S E</creatorcontrib><title>Purification and Partial Characterization of a Basic Protein from Pig Brain</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A basic protein has been isolated from pig brain. The purification procedure consisted of repeated extractions with chloroform-methanol
(2:1 v/v), 10% sodium chloride, and dilute hydrochloric acid. The pH 2.4 to 2.6 fraction obtained from the repeated acid extraction
was further purified by pH and (NH 4 ) 2 SO 4 fractionation, Sephadex G-100 gel filtration, and chromatography on Amberlite IRC-50 with a gradient (5 to 20%) of guanidinium
chloride. All of the fractions obtained by this purification procedure have been examined by starch gel electrophoresis.
The homogeneity of the pig brain basic protein has been established by ultracentrifugation, starch gel electrophoresis, polyacrylamide
gel electrophoresis, and end group analysis. Amino acid analysis performed on a complete acid hydrolysate of the protein indicated
that the ratio of basic to acidic amino acids is greater than 1.5. An absence of cysteine and the presence of a high glycine
and proline content have also been observed.</description><subject>Acrylic Resins</subject><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Brain Chemistry</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>Electrophoresis</subject><subject>Hydrogen-Ion Concentration</subject><subject>Nerve Tissue Proteins - analysis</subject><subject>Swine</subject><subject>Ultracentrifugation</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1967</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kFtLwzAYhoMoc05_wiAgiF5U8yVpm1y64QkHDlTwLqRpskbWdiYdor_e7oDfzXvxHj54EBoDuQYC2c0rIRQSSVNxCeJKSp7KJD9AQyCCJSyFj0M0_I8co5MYP0l_XMIADTKSCsnEED3P18E7b3Tn2wbrpsRzHTqvl3ha6aBNZ4P_3ZmtwxpPdPQGz0PbWd9gF9oaz_0CT4L2zSk6cnoZ7dleR-j9_u5t-pjMXh6eprezxLBcdgnXlvKMc-aEyYEDcwWxuiyl5sJK6TJT5gWjJi-5AWOgTDmTkjpqDCk0ODZCF7vdVWi_1jZ2qvbR2OVSN7ZdRyV4KoCC7IPpLmhCG2OwTq2Cr3X4UUDUBqLaQlQbQgqE2kJUed8b7x-si9qW_609td4_3_mVX1TfPlhV-NZUtlaUU9UPcskY-wP5vHjc</recordid><startdate>19671110</startdate><enddate>19671110</enddate><creator>Tomasi, L G</creator><creator>Kornguth, S E</creator><general>American Society for Biochemistry and Molecular Biology</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>19671110</creationdate><title>Purification and Partial Characterization of a Basic Protein from Pig Brain</title><author>Tomasi, L G ; Kornguth, S E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-4ae246443f8c71413fb0eadd9a48e99f6cd7b32c7d4c1cc1d543992f2cc0ba1f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1967</creationdate><topic>Acrylic Resins</topic><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Brain Chemistry</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>Electrophoresis</topic><topic>Hydrogen-Ion Concentration</topic><topic>Nerve Tissue Proteins - analysis</topic><topic>Swine</topic><topic>Ultracentrifugation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tomasi, L G</creatorcontrib><creatorcontrib>Kornguth, S E</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tomasi, L G</au><au>Kornguth, S E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Partial Characterization of a Basic Protein from Pig Brain</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1967-11-10</date><risdate>1967</risdate><volume>242</volume><issue>21</issue><spage>4933</spage><epage>4938</epage><pages>4933-4938</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A basic protein has been isolated from pig brain. The purification procedure consisted of repeated extractions with chloroform-methanol
(2:1 v/v), 10% sodium chloride, and dilute hydrochloric acid. The pH 2.4 to 2.6 fraction obtained from the repeated acid extraction
was further purified by pH and (NH 4 ) 2 SO 4 fractionation, Sephadex G-100 gel filtration, and chromatography on Amberlite IRC-50 with a gradient (5 to 20%) of guanidinium
chloride. All of the fractions obtained by this purification procedure have been examined by starch gel electrophoresis.
The homogeneity of the pig brain basic protein has been established by ultracentrifugation, starch gel electrophoresis, polyacrylamide
gel electrophoresis, and end group analysis. Amino acid analysis performed on a complete acid hydrolysate of the protein indicated
that the ratio of basic to acidic amino acids is greater than 1.5. An absence of cysteine and the presence of a high glycine
and proline content have also been observed.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>6058938</pmid><doi>10.1016/S0021-9258(18)99459-7</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1967-11, Vol.242 (21), p.4933-4938 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_84581219 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Acrylic Resins Amino Acids - analysis Animals Brain Chemistry Chromatography, Gel Chromatography, Ion Exchange Electrophoresis Hydrogen-Ion Concentration Nerve Tissue Proteins - analysis Swine Ultracentrifugation |
| title | Purification and Partial Characterization of a Basic Protein from Pig Brain |
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