A biologically active thrombin cleavage product of human serum spreading factor
Purified human serum spreading factor preparations consisting of two immunologically-related, biologically-active proteins of molecular weights approximately 65,000 and 75,000 were incubated with purified hydrolytic enzymes: papain, neuraminidase and thrombin. Biologically active products of the enz...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1984-01, Vol.118 (1), p.339-343 |
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| creator | Silnutzer, Janet Barnes, David W. |
| description | Purified human serum spreading factor preparations consisting of two immunologically-related, biologically-active proteins of molecular weights approximately 65,000 and 75,000 were incubated with purified hydrolytic enzymes: papain, neuraminidase and thrombin. Biologically active products of the enzymatic digestions were obtained in each case. Digestion of serum spreading factor preparations with thrombin produced a single active form of molecular weight approximately 57,000. Generation of a single molecular weight form of serum spreading factor by thrombin cleavage of the two higher molecular weight forms should simplify studies of the biochemistry and biology of this protein, and may represent a reaction of physiological significance. |
| doi_str_mv | 10.1016/0006-291X(84)91106-9 |
| format | Article |
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Biologically active products of the enzymatic digestions were obtained in each case. Digestion of serum spreading factor preparations with thrombin produced a single active form of molecular weight approximately 57,000. Generation of a single molecular weight form of serum spreading factor by thrombin cleavage of the two higher molecular weight forms should simplify studies of the biochemistry and biology of this protein, and may represent a reaction of physiological significance.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(84)91106-9</identifier><identifier>PMID: 6199029</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Biological Assay ; Electrophoresis, Polyacrylamide Gel ; Glycoproteins - metabolism ; Glycoproteins - pharmacology ; HeLa Cells - drug effects ; Humans ; man ; Molecular Weight ; Peptide Fragments - isolation & purification ; serum spreading factor ; thrombin ; Thrombin - metabolism ; Vitronectin</subject><ispartof>Biochemical and biophysical research communications, 1984-01, Vol.118 (1), p.339-343</ispartof><rights>1984</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-6c88a9e23d793d8ad3210c2efe063469c2572ce59d04a701b57631ee63729e733</citedby><cites>FETCH-LOGICAL-c388t-6c88a9e23d793d8ad3210c2efe063469c2572ce59d04a701b57631ee63729e733</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X84911069$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6199029$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Silnutzer, Janet</creatorcontrib><creatorcontrib>Barnes, David W.</creatorcontrib><title>A biologically active thrombin cleavage product of human serum spreading factor</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Purified human serum spreading factor preparations consisting of two immunologically-related, biologically-active proteins of molecular weights approximately 65,000 and 75,000 were incubated with purified hydrolytic enzymes: papain, neuraminidase and thrombin. Biologically active products of the enzymatic digestions were obtained in each case. Digestion of serum spreading factor preparations with thrombin produced a single active form of molecular weight approximately 57,000. Generation of a single molecular weight form of serum spreading factor by thrombin cleavage of the two higher molecular weight forms should simplify studies of the biochemistry and biology of this protein, and may represent a reaction of physiological significance.</description><subject>Biological Assay</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Glycoproteins - metabolism</subject><subject>Glycoproteins - pharmacology</subject><subject>HeLa Cells - drug effects</subject><subject>Humans</subject><subject>man</subject><subject>Molecular Weight</subject><subject>Peptide Fragments - isolation & purification</subject><subject>serum spreading factor</subject><subject>thrombin</subject><subject>Thrombin - metabolism</subject><subject>Vitronectin</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEFr3DAQhUVISLdp_0ECOoX04ERj2bJ0KSxL2gQCuSTQm5Cl8UbBtraSvZB_H213ybE5DcO89-bxEXIO7BoYiBvGmChKBX-uZPVDAeRNHZEFMMWKElh1TBYfki_ka0qvjAFUQp2SUwFKsVItyOOStj70Ye2t6fs3auzkt0inlxiG1o_U9mi2Zo10E4Ob7URDR1_mwYw0YZwHmjYRjfPjmnbZGuI3ctKZPuH3wzwjz79un1Z3xcPj7_vV8qGwXMqpEFZKo7DkrlHcSeN4bmxL7JAJnivasm5Ki7VyrDINg7ZuBAdEwZtSYcP5Gbnc5-Zef2dMkx58stj3ZsQwJy2ZEiDq-lMhcAk1SJmF1V5oY0gpYqc30Q8mvmlgegdc72jqHU0tK_0PuFbZdnHIn9sB3YfpQDjff-7vmGlsPUadrMfRovMR7aRd8P9_8A5GqI8h</recordid><startdate>19840101</startdate><enddate>19840101</enddate><creator>Silnutzer, Janet</creator><creator>Barnes, David W.</creator><general>Elsevier Inc</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19840101</creationdate><title>A biologically active thrombin cleavage product of human serum spreading factor</title><author>Silnutzer, Janet ; Barnes, David W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-6c88a9e23d793d8ad3210c2efe063469c2572ce59d04a701b57631ee63729e733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Biological Assay</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Glycoproteins - metabolism</topic><topic>Glycoproteins - pharmacology</topic><topic>HeLa Cells - drug effects</topic><topic>Humans</topic><topic>man</topic><topic>Molecular Weight</topic><topic>Peptide Fragments - isolation & purification</topic><topic>serum spreading factor</topic><topic>thrombin</topic><topic>Thrombin - metabolism</topic><topic>Vitronectin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Silnutzer, Janet</creatorcontrib><creatorcontrib>Barnes, David W.</creatorcontrib><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><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Silnutzer, Janet</au><au>Barnes, David W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A biologically active thrombin cleavage product of human serum spreading factor</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1984-01-01</date><risdate>1984</risdate><volume>118</volume><issue>1</issue><spage>339</spage><epage>343</epage><pages>339-343</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Purified human serum spreading factor preparations consisting of two immunologically-related, biologically-active proteins of molecular weights approximately 65,000 and 75,000 were incubated with purified hydrolytic enzymes: papain, neuraminidase and thrombin. Biologically active products of the enzymatic digestions were obtained in each case. Digestion of serum spreading factor preparations with thrombin produced a single active form of molecular weight approximately 57,000. Generation of a single molecular weight form of serum spreading factor by thrombin cleavage of the two higher molecular weight forms should simplify studies of the biochemistry and biology of this protein, and may represent a reaction of physiological significance.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6199029</pmid><doi>10.1016/0006-291X(84)91106-9</doi><tpages>5</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1984-01, Vol.118 (1), p.339-343 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Biological Assay Electrophoresis, Polyacrylamide Gel Glycoproteins - metabolism Glycoproteins - pharmacology HeLa Cells - drug effects Humans man Molecular Weight Peptide Fragments - isolation & purification serum spreading factor thrombin Thrombin - metabolism Vitronectin |
| title | A biologically active thrombin cleavage product of human serum spreading factor |
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