[25] Purification of rat insulin-like growth factor II
Dulak and Temin first described the purification of multiplication-stimulating activity (MSA) or rat IGF-II (rIGF-II) from serum-free medium conditioned by the BRL-3A rat liver cell line. Results of biosynthetic labeling experiments suggest that the various size rIGF-II species are derived from a co...
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| Veröffentlicht in: | Methods in Enzymology 1987, Vol.146, p.259-269 |
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| container_title | Methods in Enzymology |
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| creator | Greenstein, Lawrence A. Gaynes, Lynne A. Romanus, Joyce A. Lee, Lilly Rechler, Matthew M. Nissley, S. Peter |
| description | Dulak and Temin first described the purification of multiplication-stimulating activity (MSA) or rat IGF-II (rIGF-II) from serum-free medium conditioned by the BRL-3A rat liver cell line. Results of biosynthetic labeling experiments suggest that the various size rIGF-II species are derived from a common pro-rIGF-II (∼20 kDa). The smallest rIGF-II species (MSA-III-2) has the highest specific activity in radioreceptor assays and bioassays, and it is most easily purified to homogeneity. However, greater quantities of the 8700-Da species (MSA-II) are produced by the BRL-3A cells, and a mixture of MSA-II species can be obtained by following a two-step purification procedure. This chapter discusses the culture of the BRL-3A rat liver cell line and the measurement of rIGF-II during purification. The chapter also discusses rat IGF-II purification and evaluates rIGF-II preparations. |
| doi_str_mv | 10.1016/S0076-6879(87)46028-X |
| format | Article |
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Peter</creatorcontrib><title>[25] Purification of rat insulin-like growth factor II</title><title>Methods in Enzymology</title><addtitle>Methods Enzymol</addtitle><description>Dulak and Temin first described the purification of multiplication-stimulating activity (MSA) or rat IGF-II (rIGF-II) from serum-free medium conditioned by the BRL-3A rat liver cell line. Results of biosynthetic labeling experiments suggest that the various size rIGF-II species are derived from a common pro-rIGF-II (∼20 kDa). The smallest rIGF-II species (MSA-III-2) has the highest specific activity in radioreceptor assays and bioassays, and it is most easily purified to homogeneity. However, greater quantities of the 8700-Da species (MSA-II) are produced by the BRL-3A cells, and a mixture of MSA-II species can be obtained by following a two-step purification procedure. This chapter discusses the culture of the BRL-3A rat liver cell line and the measurement of rIGF-II during purification. The chapter also discusses rat IGF-II purification and evaluates rIGF-II preparations.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Cell Membrane - metabolism</subject><subject>Chromatography, Gel - methods</subject><subject>Chromatography, High Pressure Liquid - methods</subject><subject>Female</subject><subject>Insulin-Like Growth Factor II - isolation & purification</subject><subject>Liver - analysis</subject><subject>Placenta - metabolism</subject><subject>Radioligand Assay - methods</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Receptor, Insulin - metabolism</subject><subject>Receptors, Somatomedin</subject><subject>Somatomedins - isolation & purification</subject><issn>0076-6879</issn><issn>1557-7988</issn><isbn>0121820467</isbn><isbn>9780121820466</isbn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kN1LwzAUxYMfzDn3Jwz6JPpQTW6b3PRJZPgxGCioMBAJaZpqtGtn0ir-93ZueB_OfTiHyz0_QiaMnjHKxPkDpShiITE7kXiaCgoyXuyQIeMcY8yk3CWHlAGTQFOBe2T4nz8g4xDeaT9pBgJhQAaQCSqRDol4Bv4S3Xfelc7o1jV11JSR123k6tBVro4r92GjV998t29RqU3b-Gg2OyL7pa6CHW_3iDxdXz1Ob-P53c1sejmPTcLSNsaCI4esyCmkmmqeJoZyDiiNziwVModSYpJZzoUFLAF6sbroC7ASclMkI3K8ubvyzWdnQ6uWLhhbVbq2TRcUokwkcOyDk22wy5e2UCvvltr_qG3R3r_Y-Lb_9stZr4Jxtja2cN6aVhWNU4yqNWn1R1qtySmJ6o-0WiS_HyVrNQ</recordid><startdate>1987</startdate><enddate>1987</enddate><creator>Greenstein, Lawrence A.</creator><creator>Gaynes, Lynne A.</creator><creator>Romanus, Joyce A.</creator><creator>Lee, Lilly</creator><creator>Rechler, Matthew M.</creator><creator>Nissley, S. 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Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c314t-7d57529db024a0a543c055278ca9e068b2f8739e556e27f2227fead0461f2bcd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Cell Membrane - metabolism</topic><topic>Chromatography, Gel - methods</topic><topic>Chromatography, High Pressure Liquid - methods</topic><topic>Female</topic><topic>Insulin-Like Growth Factor II - isolation & purification</topic><topic>Liver - analysis</topic><topic>Placenta - metabolism</topic><topic>Radioligand Assay - methods</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Receptor, Insulin - metabolism</topic><topic>Receptors, Somatomedin</topic><topic>Somatomedins - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Greenstein, Lawrence A.</creatorcontrib><creatorcontrib>Gaynes, Lynne A.</creatorcontrib><creatorcontrib>Romanus, Joyce A.</creatorcontrib><creatorcontrib>Lee, Lilly</creatorcontrib><creatorcontrib>Rechler, Matthew M.</creatorcontrib><creatorcontrib>Nissley, S. Peter</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Methods in Enzymology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Greenstein, Lawrence A.</au><au>Gaynes, Lynne A.</au><au>Romanus, Joyce A.</au><au>Lee, Lilly</au><au>Rechler, Matthew M.</au><au>Nissley, S. Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>[25] Purification of rat insulin-like growth factor II</atitle><jtitle>Methods in Enzymology</jtitle><addtitle>Methods Enzymol</addtitle><date>1987</date><risdate>1987</risdate><volume>146</volume><spage>259</spage><epage>269</epage><pages>259-269</pages><issn>0076-6879</issn><eissn>1557-7988</eissn><isbn>0121820467</isbn><isbn>9780121820466</isbn><abstract>Dulak and Temin first described the purification of multiplication-stimulating activity (MSA) or rat IGF-II (rIGF-II) from serum-free medium conditioned by the BRL-3A rat liver cell line. Results of biosynthetic labeling experiments suggest that the various size rIGF-II species are derived from a common pro-rIGF-II (∼20 kDa). The smallest rIGF-II species (MSA-III-2) has the highest specific activity in radioreceptor assays and bioassays, and it is most easily purified to homogeneity. However, greater quantities of the 8700-Da species (MSA-II) are produced by the BRL-3A cells, and a mixture of MSA-II species can be obtained by following a two-step purification procedure. This chapter discusses the culture of the BRL-3A rat liver cell line and the measurement of rIGF-II during purification. The chapter also discusses rat IGF-II purification and evaluates rIGF-II preparations.</abstract><cop>United States</cop><pub>Elsevier Science & Technology</pub><pmid>2960870</pmid><doi>10.1016/S0076-6879(87)46028-X</doi><tpages>11</tpages></addata></record> |
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| ispartof | Methods in Enzymology, 1987, Vol.146, p.259-269 |
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| language | eng |
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| source | ScienceDirect eBooks; MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Cell Line Cell Membrane - metabolism Chromatography, Gel - methods Chromatography, High Pressure Liquid - methods Female Insulin-Like Growth Factor II - isolation & purification Liver - analysis Placenta - metabolism Radioligand Assay - methods Rats Rats, Inbred Strains Receptor, Insulin - metabolism Receptors, Somatomedin Somatomedins - isolation & purification |
| title | [25] Purification of rat insulin-like growth factor II |
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