Isolation and partial characterization of bovine and equine factor D
Bovine and equine factor D were purified to apparent homogeneity as evidenced by a single protein staining band on 7.5–17.5% SDS-PAGE slab gels under both reducing and non-reducing conditions. An apparent mol. wt of 15,000 for bovine D and 22,500 for equine D were noted after SDS-PAGE gel analysis o...
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| Veröffentlicht in: | Molecular immunology 1984-01, Vol.21 (10), p.869-876 |
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| container_title | Molecular immunology |
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| creator | Blanchard, D.B. Leid, R.Wes |
| description | Bovine and equine factor D were purified to apparent homogeneity as evidenced by a single protein staining band on 7.5–17.5% SDS-PAGE slab gels under both reducing and non-reducing conditions. An apparent mol. wt of 15,000 for bovine D and 22,500 for equine D were noted after SDS-PAGE gel analysis of both reduced and non-reduced preparations. A single polypeptide chain for both proteins was evidenced by the lack of any change in the electrophoretic mobility under each of these conditions. The bovine and equine D were enriched 3347- and 9447-fold, with a 20 and 29% yield of hemolytic activity, respectively. Functionally, both equine and bovine D would reconstitute a human reagent deficient in D (RD), while human or equine D would substitute for bovine D when using a bovine RD. Neither bovine, equine or human D would, however, reconstitute an equine RD. |
| doi_str_mv | 10.1016/0161-5890(84)90141-X |
| format | Article |
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An apparent mol. wt of 15,000 for bovine D and 22,500 for equine D were noted after SDS-PAGE gel analysis of both reduced and non-reduced preparations. A single polypeptide chain for both proteins was evidenced by the lack of any change in the electrophoretic mobility under each of these conditions. The bovine and equine D were enriched 3347- and 9447-fold, with a 20 and 29% yield of hemolytic activity, respectively. Functionally, both equine and bovine D would reconstitute a human reagent deficient in D (RD), while human or equine D would substitute for bovine D when using a bovine RD. 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An apparent mol. wt of 15,000 for bovine D and 22,500 for equine D were noted after SDS-PAGE gel analysis of both reduced and non-reduced preparations. A single polypeptide chain for both proteins was evidenced by the lack of any change in the electrophoretic mobility under each of these conditions. The bovine and equine D were enriched 3347- and 9447-fold, with a 20 and 29% yield of hemolytic activity, respectively. Functionally, both equine and bovine D would reconstitute a human reagent deficient in D (RD), while human or equine D would substitute for bovine D when using a bovine RD. Neither bovine, equine or human D would, however, reconstitute an equine RD.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>cattle</subject><subject>Cattle - immunology</subject><subject>Chromatography</subject><subject>Complement</subject><subject>Complement Activating Enzymes - isolation & purification</subject><subject>complement factor D</subject><subject>Complement Factor D - isolation & purification</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>factor D</subject><subject>Fibrinogen</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Hemolysis</subject><subject>horses</subject><subject>Horses - immunology</subject><subject>Molecular immunology</subject><subject>Molecular Weight</subject><issn>0161-5890</issn><issn>1872-9142</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMotVb_gcIeRPSwmtnNJtmLIK0fhYIXhd5CNptgZLupybagv960W3rUwzAD7zPD8CB0DvgWMNC7WJAWvMTXnNyUGAik8wM0BM6ytASSHaLhHjlGJyF8YowppsUADWhBOQE8RJNpcI3srGsT2dbJUvrOyiZRH9JL1Wlvf_rQmaRya9vqLaa_VpvRRMT5ZHKKjoxsgj7b9RF6f3p8G7-ks9fn6fhhlioCrEsBTK7AEK6AqDIHpphhStdVRrXhWQ00N4YrY2osiziyjFfAdc6KCCpJ8xG66u8uvfta6dCJhQ1KN41stVsFwQrGOOTZv2B0BXleFBEkPai8C8FrI5beLqT_FoDFxrLYKBQbhYITsbUs5nHtYnd_VS10vV_aaY355S6XQcnGeNkqG_ZYCUDZFrvvMR2lra32Iiir26jEeq06UTv79x-_gMCYpg</recordid><startdate>19840101</startdate><enddate>19840101</enddate><creator>Blanchard, D.B.</creator><creator>Leid, R.Wes</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</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>7X8</scope></search><sort><creationdate>19840101</creationdate><title>Isolation and partial characterization of bovine and equine factor D</title><author>Blanchard, D.B. ; Leid, R.Wes</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-11f3c1f48c14c9317c7f7cedb26ef82d163ff8cffd0a53ff728b18e375c7fca63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>cattle</topic><topic>Cattle - immunology</topic><topic>Chromatography</topic><topic>Complement</topic><topic>Complement Activating Enzymes - isolation & purification</topic><topic>complement factor D</topic><topic>Complement Factor D - isolation & purification</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>factor D</topic><topic>Fibrinogen</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Hemolysis</topic><topic>horses</topic><topic>Horses - immunology</topic><topic>Molecular immunology</topic><topic>Molecular Weight</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Blanchard, D.B.</creatorcontrib><creatorcontrib>Leid, R.Wes</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Blanchard, D.B.</au><au>Leid, R.Wes</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and partial characterization of bovine and equine factor D</atitle><jtitle>Molecular immunology</jtitle><addtitle>Mol Immunol</addtitle><date>1984-01-01</date><risdate>1984</risdate><volume>21</volume><issue>10</issue><spage>869</spage><epage>876</epage><pages>869-876</pages><issn>0161-5890</issn><eissn>1872-9142</eissn><coden>MOIMD5</coden><abstract>Bovine and equine factor D were purified to apparent homogeneity as evidenced by a single protein staining band on 7.5–17.5% SDS-PAGE slab gels under both reducing and non-reducing conditions. An apparent mol. wt of 15,000 for bovine D and 22,500 for equine D were noted after SDS-PAGE gel analysis of both reduced and non-reduced preparations. A single polypeptide chain for both proteins was evidenced by the lack of any change in the electrophoretic mobility under each of these conditions. The bovine and equine D were enriched 3347- and 9447-fold, with a 20 and 29% yield of hemolytic activity, respectively. Functionally, both equine and bovine D would reconstitute a human reagent deficient in D (RD), while human or equine D would substitute for bovine D when using a bovine RD. Neither bovine, equine or human D would, however, reconstitute an equine RD.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>6568410</pmid><doi>10.1016/0161-5890(84)90141-X</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0161-5890 |
| ispartof | Molecular immunology, 1984-01, Vol.21 (10), p.869-876 |
| issn | 0161-5890 1872-9142 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Biological and medical sciences cattle Cattle - immunology Chromatography Complement Complement Activating Enzymes - isolation & purification complement factor D Complement Factor D - isolation & purification Electrophoresis, Polyacrylamide Gel factor D Fibrinogen Fundamental and applied biological sciences. Psychology Fundamental immunology Hemolysis horses Horses - immunology Molecular immunology Molecular Weight |
| title | Isolation and partial characterization of bovine and equine factor D |
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