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Partial purification and characterization of a growth factor present in goat's colostrum. Similarities with platelet-derived growth factor
A factor in goat's colostrum which stimulates DNA synthesis and cell proliferation in Swiss 3T3 fibroblasts has been purified approx. 350-fold by a sequence of acid precipitation, cation-exchange chromatography and gel filtration. The growth factor is a highly basic, heat stable (100 degrees C...
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Published in: | Biochemical journal 1984-04, Vol.219 (2), p.609-617 |
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description | A factor in goat's colostrum which stimulates DNA synthesis and cell proliferation in Swiss 3T3 fibroblasts has been purified approx. 350-fold by a sequence of acid precipitation, cation-exchange chromatography and gel filtration. The growth factor is a highly basic, heat stable (100 degrees C for 5 min) polypeptide with Mr approx. 35000. The polypeptide resists denaturation by guanidinium chloride or urea but is totally inactivated by treatment with reducing agents. The factor, which we have termed colostric basic growth factor ( CBGF ), inhibits the binding of 125I-labelled epidermal growth factor (125I-EGF) to Swiss 3T3 fibroblasts but does not inhibit 125I-EGF binding to epidermoid A431 cells. CBGF interacts synergistically with plasma in stimulating DNA synthesis in quiescent Swiss 3T3 cells. The chemical and biological properties of CBGF are thus very similar to the properties reported for the human platelet-derived growth factor. Although high concentrations of CBGF are present in the colostrum of goats, cows, and sheep, the milk of these species contains little or no factor. The origin and possible functions of CBGF are unknown. |
doi_str_mv | 10.1042/bj2190609 |
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Similarities with platelet-derived growth factor</title><source>PubMed</source><creator>Brown, K.D ; Blakeley, D.M</creator><creatorcontrib>Brown, K.D ; Blakeley, D.M</creatorcontrib><description>A factor in goat's colostrum which stimulates DNA synthesis and cell proliferation in Swiss 3T3 fibroblasts has been purified approx. 350-fold by a sequence of acid precipitation, cation-exchange chromatography and gel filtration. The growth factor is a highly basic, heat stable (100 degrees C for 5 min) polypeptide with Mr approx. 35000. The polypeptide resists denaturation by guanidinium chloride or urea but is totally inactivated by treatment with reducing agents. The factor, which we have termed colostric basic growth factor ( CBGF ), inhibits the binding of 125I-labelled epidermal growth factor (125I-EGF) to Swiss 3T3 fibroblasts but does not inhibit 125I-EGF binding to epidermoid A431 cells. CBGF interacts synergistically with plasma in stimulating DNA synthesis in quiescent Swiss 3T3 cells. The chemical and biological properties of CBGF are thus very similar to the properties reported for the human platelet-derived growth factor. Although high concentrations of CBGF are present in the colostrum of goats, cows, and sheep, the milk of these species contains little or no factor. The origin and possible functions of CBGF are unknown.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2190609</identifier><identifier>PMID: 6378177</identifier><language>eng</language><publisher>England</publisher><subject>animal physiology ; Animals ; Cell Division - drug effects ; Cell Line ; Chromatography, Gel ; Chromatography, Ion Exchange ; colostrum ; Colostrum - analysis ; Cricetinae ; DNA - biosynthesis ; Epidermal Growth Factor - metabolism ; Female ; Fibroblasts - drug effects ; Goats ; growth factors ; Growth Substances - analysis ; Growth Substances - isolation & purification ; Growth Substances - pharmacology ; man ; Milk Proteins ; Oxidation-Reduction ; Peptide Hydrolases - pharmacology ; platelet-derived growth factor ; Protein Denaturation</subject><ispartof>Biochemical journal, 1984-04, Vol.219 (2), p.609-617</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425t-e897cd8611da277dcb954e850ee6cec7c5dd613deb76c77b5d132a19b8cd74cf3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1153519/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1153519/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6378177$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brown, K.D</creatorcontrib><creatorcontrib>Blakeley, D.M</creatorcontrib><title>Partial purification and characterization of a growth factor present in goat's colostrum. Similarities with platelet-derived growth factor</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>A factor in goat's colostrum which stimulates DNA synthesis and cell proliferation in Swiss 3T3 fibroblasts has been purified approx. 350-fold by a sequence of acid precipitation, cation-exchange chromatography and gel filtration. The growth factor is a highly basic, heat stable (100 degrees C for 5 min) polypeptide with Mr approx. 35000. The polypeptide resists denaturation by guanidinium chloride or urea but is totally inactivated by treatment with reducing agents. The factor, which we have termed colostric basic growth factor ( CBGF ), inhibits the binding of 125I-labelled epidermal growth factor (125I-EGF) to Swiss 3T3 fibroblasts but does not inhibit 125I-EGF binding to epidermoid A431 cells. CBGF interacts synergistically with plasma in stimulating DNA synthesis in quiescent Swiss 3T3 cells. The chemical and biological properties of CBGF are thus very similar to the properties reported for the human platelet-derived growth factor. Although high concentrations of CBGF are present in the colostrum of goats, cows, and sheep, the milk of these species contains little or no factor. The origin and possible functions of CBGF are unknown.</description><subject>animal physiology</subject><subject>Animals</subject><subject>Cell Division - drug effects</subject><subject>Cell Line</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>colostrum</subject><subject>Colostrum - analysis</subject><subject>Cricetinae</subject><subject>DNA - biosynthesis</subject><subject>Epidermal Growth Factor - metabolism</subject><subject>Female</subject><subject>Fibroblasts - drug effects</subject><subject>Goats</subject><subject>growth factors</subject><subject>Growth Substances - analysis</subject><subject>Growth Substances - isolation & purification</subject><subject>Growth Substances - pharmacology</subject><subject>man</subject><subject>Milk Proteins</subject><subject>Oxidation-Reduction</subject><subject>Peptide Hydrolases - pharmacology</subject><subject>platelet-derived growth factor</subject><subject>Protein Denaturation</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><recordid>eNqFkcFqFTEUhoMo9ba68AHErBQXU3OSzCSzEaRYFQoKteuQSc7cmzIzGZNMiz6CT-3IvVzsytWB83_5OOEn5AWwc2CSv-tuObSsYe0jsgGpWKUV14_JhvFGVg3j8JSc5nzLGEgm2Qk5aYTSoNSG_P5mUwl2oPOSQh-cLSFO1E6eup1N1hVM4dd-GXtq6TbF-7Kj_ZrEROeEGadCw0S30ZY3mbo4xFzSMp7T6zCGwaZQAmZ6H9ZX82ALDlgqv1rv0D-0PSNPejtkfH6YZ-Tm8uP3i8_V1ddPXy4-XFVO8rpUqFvlvG4AvOVKede1tURdM8TGoVOu9r4B4bFTjVOqqz0IbqHttPNKul6ckfd777x0I3q3fiDZwcwpjDb9NNEG8zCZws5s450BqEUN7Sp4fRCk-GPBXMwYssNhsBPGJRu9glK18F8QhJZKKL6Cb_egSzHnhP3xGmDmb8Pm2PDKvvz3_CN5qHTNX-3z3kZjtylkc3PNGQjG60ZwLcQfqW2vVA</recordid><startdate>19840415</startdate><enddate>19840415</enddate><creator>Brown, K.D</creator><creator>Blakeley, D.M</creator><scope>FBQ</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>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19840415</creationdate><title>Partial purification and characterization of a growth factor present in goat's colostrum. Similarities with platelet-derived growth factor</title><author>Brown, K.D ; Blakeley, D.M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c425t-e897cd8611da277dcb954e850ee6cec7c5dd613deb76c77b5d132a19b8cd74cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>animal physiology</topic><topic>Animals</topic><topic>Cell Division - drug effects</topic><topic>Cell Line</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>colostrum</topic><topic>Colostrum - analysis</topic><topic>Cricetinae</topic><topic>DNA - biosynthesis</topic><topic>Epidermal Growth Factor - metabolism</topic><topic>Female</topic><topic>Fibroblasts - drug effects</topic><topic>Goats</topic><topic>growth factors</topic><topic>Growth Substances - analysis</topic><topic>Growth Substances - isolation & purification</topic><topic>Growth Substances - pharmacology</topic><topic>man</topic><topic>Milk Proteins</topic><topic>Oxidation-Reduction</topic><topic>Peptide Hydrolases - pharmacology</topic><topic>platelet-derived growth factor</topic><topic>Protein Denaturation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brown, K.D</creatorcontrib><creatorcontrib>Blakeley, D.M</creatorcontrib><collection>AGRIS</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>Environmental Sciences and Pollution Management</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>Brown, K.D</au><au>Blakeley, D.M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Partial purification and characterization of a growth factor present in goat's colostrum. Similarities with platelet-derived growth factor</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1984-04-15</date><risdate>1984</risdate><volume>219</volume><issue>2</issue><spage>609</spage><epage>617</epage><pages>609-617</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>A factor in goat's colostrum which stimulates DNA synthesis and cell proliferation in Swiss 3T3 fibroblasts has been purified approx. 350-fold by a sequence of acid precipitation, cation-exchange chromatography and gel filtration. The growth factor is a highly basic, heat stable (100 degrees C for 5 min) polypeptide with Mr approx. 35000. The polypeptide resists denaturation by guanidinium chloride or urea but is totally inactivated by treatment with reducing agents. The factor, which we have termed colostric basic growth factor ( CBGF ), inhibits the binding of 125I-labelled epidermal growth factor (125I-EGF) to Swiss 3T3 fibroblasts but does not inhibit 125I-EGF binding to epidermoid A431 cells. CBGF interacts synergistically with plasma in stimulating DNA synthesis in quiescent Swiss 3T3 cells. The chemical and biological properties of CBGF are thus very similar to the properties reported for the human platelet-derived growth factor. Although high concentrations of CBGF are present in the colostrum of goats, cows, and sheep, the milk of these species contains little or no factor. The origin and possible functions of CBGF are unknown.</abstract><cop>England</cop><pmid>6378177</pmid><doi>10.1042/bj2190609</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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subjects | animal physiology Animals Cell Division - drug effects Cell Line Chromatography, Gel Chromatography, Ion Exchange colostrum Colostrum - analysis Cricetinae DNA - biosynthesis Epidermal Growth Factor - metabolism Female Fibroblasts - drug effects Goats growth factors Growth Substances - analysis Growth Substances - isolation & purification Growth Substances - pharmacology man Milk Proteins Oxidation-Reduction Peptide Hydrolases - pharmacology platelet-derived growth factor Protein Denaturation |
title | Partial purification and characterization of a growth factor present in goat's colostrum. Similarities with platelet-derived growth factor |
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