Solubilization of IgG-Binding Proteins from Group A and G Streptococci
The release of IgG-binding proteins from the cell surface of streptococcal strains AR-1 and G148 with various proteolytic enzymes, acid, alkali or SDS was investigated. The IgG-binding proteins were purified by affinity chromatography using IgG-Sepharose Fast Flow. After SDS-polyacrylamide gel elect...
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| Veröffentlicht in: | MICROBIOLOGY and IMMUNOLOGY 1989, Vol.33(2), pp.123-127 |
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| container_issue | 2 |
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| container_title | MICROBIOLOGY and IMMUNOLOGY |
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| creator | Goward, Christopher R. Barstow, David A. |
| description | The release of IgG-binding proteins from the cell surface of streptococcal strains AR-1 and G148 with various proteolytic enzymes, acid, alkali or SDS was investigated. The IgG-binding proteins were purified by affinity chromatography using IgG-Sepharose Fast Flow. After SDS-polyacrylamide gel electrophoresis and immuno-electroblotting the major proteins identified varied in relative molecular mass from 15, 000 to 65, 000 depending on the solubilizing agent used. The results showed that solubilization with trypsin gave the highest yield of IgG-binding proteins, that strain G148 yielded about twice the amount of protein as strain AR-1, and that elastase released an IgG-binding protein of high relative molecular mass of 65, 000. |
| doi_str_mv | 10.1111/j.1348-0421.1989.tb01504.x |
| format | Article |
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The IgG-binding proteins were purified by affinity chromatography using IgG-Sepharose Fast Flow. After SDS-polyacrylamide gel electrophoresis and immuno-electroblotting the major proteins identified varied in relative molecular mass from 15, 000 to 65, 000 depending on the solubilizing agent used. The results showed that solubilization with trypsin gave the highest yield of IgG-binding proteins, that strain G148 yielded about twice the amount of protein as strain AR-1, and that elastase released an IgG-binding protein of high relative molecular mass of 65, 000.</description><identifier>ISSN: 0385-5600</identifier><identifier>EISSN: 1348-0421</identifier><identifier>DOI: 10.1111/j.1348-0421.1989.tb01504.x</identifier><identifier>PMID: 2654575</identifier><language>eng</language><publisher>Australia: Blackwell Publishing Ltd</publisher><subject>Bacterial Proteins - isolation & purification ; cell surface ; Immunoglobulin G ; immunoglobulin G-binding protein ; Membrane Proteins - isolation & purification ; Molecular Weight ; Pancreatic Elastase ; Solubility ; solubilization ; Streptococcus ; Streptococcus - analysis ; Streptococcus - classification ; Streptococcus group G ; Streptococcus pyogenes ; Streptococcus pyogenes - analysis ; Trypsin</subject><ispartof>MICROBIOLOGY and IMMUNOLOGY, 1989, Vol.33(2), pp.123-127</ispartof><rights>Center for Academic Publications Japan</rights><rights>owned by Center for Academic Publications Japan (Publisher)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5234-19b3cc899a7de0fa3e3a07144825fee56479d1b7724741730b72523516d0aeef3</citedby><cites>FETCH-LOGICAL-c5234-19b3cc899a7de0fa3e3a07144825fee56479d1b7724741730b72523516d0aeef3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1882,4023,27922,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2654575$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Goward, Christopher R.</creatorcontrib><creatorcontrib>Barstow, David A.</creatorcontrib><title>Solubilization of IgG-Binding Proteins from Group A and G Streptococci</title><title>MICROBIOLOGY and IMMUNOLOGY</title><addtitle>Microbiology and Immunology</addtitle><description>The release of IgG-binding proteins from the cell surface of streptococcal strains AR-1 and G148 with various proteolytic enzymes, acid, alkali or SDS was investigated. The IgG-binding proteins were purified by affinity chromatography using IgG-Sepharose Fast Flow. After SDS-polyacrylamide gel electrophoresis and immuno-electroblotting the major proteins identified varied in relative molecular mass from 15, 000 to 65, 000 depending on the solubilizing agent used. The results showed that solubilization with trypsin gave the highest yield of IgG-binding proteins, that strain G148 yielded about twice the amount of protein as strain AR-1, and that elastase released an IgG-binding protein of high relative molecular mass of 65, 000.</description><subject>Bacterial Proteins - isolation & purification</subject><subject>cell surface</subject><subject>Immunoglobulin G</subject><subject>immunoglobulin G-binding protein</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Molecular Weight</subject><subject>Pancreatic Elastase</subject><subject>Solubility</subject><subject>solubilization</subject><subject>Streptococcus</subject><subject>Streptococcus - analysis</subject><subject>Streptococcus - classification</subject><subject>Streptococcus group G</subject><subject>Streptococcus pyogenes</subject><subject>Streptococcus pyogenes - analysis</subject><subject>Trypsin</subject><issn>0385-5600</issn><issn>1348-0421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkV1v0zAYhS0EGqXwE5AiLtBuEvwZx1yxTWtWsfGhgiZxYzmOU1ySuNiJ1u3X45Kq4gqEL2xL57zPkd4DwCsEMxTPm02GCC1SSDHKkChENlQQMUiz3SMwO0qPwQySgqUsh_ApeBbCBkLMcUFPwAnOGWWczcBi5dqxsq19UIN1feKaZLku03Pb17ZfJ5-8G4ztQ9J41yWld-M2OUtUXydlshq82Q5OO63tc_CkUW0wLw7vHHxdXH65uEqvP5bLi7PrVDNMaIpERbQuhFC8NrBRxBAFOaK0wKwxhuWUixpVnGPKKeIEVhzHQYbyGipjGjIHryfu1rufowmD7GzQpm1Vb9wYJC8EFzln_zQihmJIjJiD078bqcA5gjTfW99OVu1dCN40cuttp_y9RFDui5Ebud--3G9f7ouRh2LkLg6_POSMVWfq4-ihiai_m_Q725r7_yDLm-XN729EXE6ITRjU2hwZyg9Wt0Z2sTeLBOeSEImnC2Fy1PV35aXpIyedODYMZvcH5oeMW-BM3n4o5WJ19f728zcqz8kvrezDXQ</recordid><startdate>1989</startdate><enddate>1989</enddate><creator>Goward, Christopher R.</creator><creator>Barstow, David A.</creator><general>Blackwell Publishing Ltd</general><general>Center For Academic Publications Japan</general><scope>BSCLL</scope><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>7QL</scope><scope>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>8FD</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>1989</creationdate><title>Solubilization of IgG-Binding Proteins from Group A and G Streptococci</title><author>Goward, Christopher R. ; 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The IgG-binding proteins were purified by affinity chromatography using IgG-Sepharose Fast Flow. After SDS-polyacrylamide gel electrophoresis and immuno-electroblotting the major proteins identified varied in relative molecular mass from 15, 000 to 65, 000 depending on the solubilizing agent used. The results showed that solubilization with trypsin gave the highest yield of IgG-binding proteins, that strain G148 yielded about twice the amount of protein as strain AR-1, and that elastase released an IgG-binding protein of high relative molecular mass of 65, 000.</abstract><cop>Australia</cop><pub>Blackwell Publishing Ltd</pub><pmid>2654575</pmid><doi>10.1111/j.1348-0421.1989.tb01504.x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0385-5600 |
| ispartof | MICROBIOLOGY and IMMUNOLOGY, 1989, Vol.33(2), pp.123-127 |
| issn | 0385-5600 1348-0421 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78979675 |
| source | J-STAGE Free; MEDLINE; Freely Accessible Japanese Titles; Alma/SFX Local Collection |
| subjects | Bacterial Proteins - isolation & purification cell surface Immunoglobulin G immunoglobulin G-binding protein Membrane Proteins - isolation & purification Molecular Weight Pancreatic Elastase Solubility solubilization Streptococcus Streptococcus - analysis Streptococcus - classification Streptococcus group G Streptococcus pyogenes Streptococcus pyogenes - analysis Trypsin |
| title | Solubilization of IgG-Binding Proteins from Group A and G Streptococci |
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