Purification, Characterization and Antitumor Activity of Rana nigromaculata Lectin
The lectin from Rana nigromaculata eggs was isolated by Sephadex G-75 gel filtration, DEAE-cellulose and Hydroxylapatite column chromatography. Isolated lectin was obtained in a homogeneous state by polyacrylamide gel electrophoresis (PAGE), and characterized as a basic protein with a molecular weig...
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| Veröffentlicht in: | YAKUGAKU ZASSHI 1980/07/25, Vol.100(7), pp.706-712 |
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| container_title | YAKUGAKU ZASSHI |
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| creator | SUE, HIROSHI TAKAYANAGI, GIICHI KOSEKI, TOMOKO NITTA, KAZUO SAKAKIBARA, FUSAO KAWAUCHI, HIROAKI |
| description | The lectin from Rana nigromaculata eggs was isolated by Sephadex G-75 gel filtration, DEAE-cellulose and Hydroxylapatite column chromatography. Isolated lectin was obtained in a homogeneous state by polyacrylamide gel electrophoresis (PAGE), and characterized as a basic protein with a molecular weight of 15500 by SDS-PAGE and an isoelectric point of pH 9.6 by isoelectric focusing. Amino acid analysis revealed threonine, aspartic acid, serine and qlutamic acid to be the predominant amino acids, the basic amino acids were relatively little. The isolated lectin strongly agglutinated cancer cells from experimental animals. The minimum agglutinating dose of lectin was 2.0 μg/0.2 ml for Ehrlich ascites carcinoma cells and 0.5 μg/0.2 ml for ascites hepatoma 109A cells. Agglutination it was specifically inhibited by ganglioside of human erythrocytes. This lectin strongly inhibited the growth of ascitic Ehrlich carcinoma while it was less active against the solid type. |
| doi_str_mv | 10.1248/yakushi1947.100.7_706 |
| format | Article |
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Isolated lectin was obtained in a homogeneous state by polyacrylamide gel electrophoresis (PAGE), and characterized as a basic protein with a molecular weight of 15500 by SDS-PAGE and an isoelectric point of pH 9.6 by isoelectric focusing. Amino acid analysis revealed threonine, aspartic acid, serine and qlutamic acid to be the predominant amino acids, the basic amino acids were relatively little. The isolated lectin strongly agglutinated cancer cells from experimental animals. The minimum agglutinating dose of lectin was 2.0 μg/0.2 ml for Ehrlich ascites carcinoma cells and 0.5 μg/0.2 ml for ascites hepatoma 109A cells. Agglutination it was specifically inhibited by ganglioside of human erythrocytes. This lectin strongly inhibited the growth of ascitic Ehrlich carcinoma while it was less active against the solid type.</description><identifier>ISSN: 0031-6903</identifier><identifier>EISSN: 1347-5231</identifier><identifier>DOI: 10.1248/yakushi1947.100.7_706</identifier><identifier>PMID: 7193723</identifier><language>eng ; jpn</language><publisher>Japan: The Pharmaceutical Society of Japan</publisher><subject>Agglutination - drug effects ; Animals ; Antineoplastic Agents - isolation & purification ; antitumor ; basic protein ; Chemical Phenomena ; Chemistry, Physical ; Female ; frog eggs ; ganglioside ; Humans ; lectin ; Lectins - isolation & purification ; Lectins - pharmacology ; Male ; Mice ; Ovum - analysis ; rana nigromaculata nigromaculata hallowell ; Ranidae ; Rats</subject><ispartof>YAKUGAKU ZASSHI, 1980/07/25, Vol.100(7), pp.706-712</ispartof><rights>by the PHARMACEUTICAL SOCIETY OF JAPAN</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3326-fc9f9913b9a5b0b1d3e29602afe0106924e0a80f87370726f28ee9c91e2cf3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1883,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7193723$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SUE, HIROSHI</creatorcontrib><creatorcontrib>TAKAYANAGI, GIICHI</creatorcontrib><creatorcontrib>KOSEKI, TOMOKO</creatorcontrib><creatorcontrib>NITTA, KAZUO</creatorcontrib><creatorcontrib>SAKAKIBARA, FUSAO</creatorcontrib><creatorcontrib>KAWAUCHI, HIROAKI</creatorcontrib><title>Purification, Characterization and Antitumor Activity of Rana nigromaculata Lectin</title><title>YAKUGAKU ZASSHI</title><addtitle>YAKUGAKU ZASSHI</addtitle><description>The lectin from Rana nigromaculata eggs was isolated by Sephadex G-75 gel filtration, DEAE-cellulose and Hydroxylapatite column chromatography. Isolated lectin was obtained in a homogeneous state by polyacrylamide gel electrophoresis (PAGE), and characterized as a basic protein with a molecular weight of 15500 by SDS-PAGE and an isoelectric point of pH 9.6 by isoelectric focusing. Amino acid analysis revealed threonine, aspartic acid, serine and qlutamic acid to be the predominant amino acids, the basic amino acids were relatively little. The isolated lectin strongly agglutinated cancer cells from experimental animals. The minimum agglutinating dose of lectin was 2.0 μg/0.2 ml for Ehrlich ascites carcinoma cells and 0.5 μg/0.2 ml for ascites hepatoma 109A cells. Agglutination it was specifically inhibited by ganglioside of human erythrocytes. This lectin strongly inhibited the growth of ascitic Ehrlich carcinoma while it was less active against the solid type.</description><subject>Agglutination - drug effects</subject><subject>Animals</subject><subject>Antineoplastic Agents - isolation & purification</subject><subject>antitumor</subject><subject>basic protein</subject><subject>Chemical Phenomena</subject><subject>Chemistry, Physical</subject><subject>Female</subject><subject>frog eggs</subject><subject>ganglioside</subject><subject>Humans</subject><subject>lectin</subject><subject>Lectins - isolation & purification</subject><subject>Lectins - pharmacology</subject><subject>Male</subject><subject>Mice</subject><subject>Ovum - analysis</subject><subject>rana nigromaculata nigromaculata hallowell</subject><subject>Ranidae</subject><subject>Rats</subject><issn>0031-6903</issn><issn>1347-5231</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkE1rGzEQhkVpcUyanxDYU05ddyTtrlZHY5rUYGgwvYtZeRSr3Q9X0hacX5-tbUwOncvAvB8DD2P3HBZcFPXXI_4e495zXagFB1goo6D6wOZcFiovheQf2RxA8rzSIG_YXYy-ARDTlLyesZniWioh52z7PAbvvMXkh_5LttpjQJso-NfTJcN-ly375NPYDSFb2uT_-nTMBpdtsces9y9h6NCOLSbMNjTp_Wf2yWEb6e6yb9n28dvP1fd88-NpvVpuciulqHJntdOay0Zj2UDDd5KErkCgI-BQaVEQYA2uVlKBEpUTNZG2mpOwTt6yh3PpIQx_RorJdD5aalvsaRijUWVRKdDVZCzPRhuGGAM5cwi-w3A0HMw_luYdy-kG5sRyyt1fHoxNR7tr6kJu0tdn_VdM-EJXHUPytqX_tF67rx470TbUyzcC-oyB</recordid><startdate>198007</startdate><enddate>198007</enddate><creator>SUE, HIROSHI</creator><creator>TAKAYANAGI, GIICHI</creator><creator>KOSEKI, TOMOKO</creator><creator>NITTA, KAZUO</creator><creator>SAKAKIBARA, FUSAO</creator><creator>KAWAUCHI, HIROAKI</creator><general>The Pharmaceutical Society of Japan</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>7X8</scope></search><sort><creationdate>198007</creationdate><title>Purification, Characterization and Antitumor Activity of Rana nigromaculata Lectin</title><author>SUE, HIROSHI ; TAKAYANAGI, GIICHI ; KOSEKI, TOMOKO ; NITTA, KAZUO ; SAKAKIBARA, FUSAO ; KAWAUCHI, HIROAKI</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3326-fc9f9913b9a5b0b1d3e29602afe0106924e0a80f87370726f28ee9c91e2cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng ; jpn</language><creationdate>1980</creationdate><topic>Agglutination - drug effects</topic><topic>Animals</topic><topic>Antineoplastic Agents - isolation & purification</topic><topic>antitumor</topic><topic>basic protein</topic><topic>Chemical Phenomena</topic><topic>Chemistry, Physical</topic><topic>Female</topic><topic>frog eggs</topic><topic>ganglioside</topic><topic>Humans</topic><topic>lectin</topic><topic>Lectins - isolation & purification</topic><topic>Lectins - pharmacology</topic><topic>Male</topic><topic>Mice</topic><topic>Ovum - analysis</topic><topic>rana nigromaculata nigromaculata hallowell</topic><topic>Ranidae</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SUE, HIROSHI</creatorcontrib><creatorcontrib>TAKAYANAGI, GIICHI</creatorcontrib><creatorcontrib>KOSEKI, TOMOKO</creatorcontrib><creatorcontrib>NITTA, KAZUO</creatorcontrib><creatorcontrib>SAKAKIBARA, FUSAO</creatorcontrib><creatorcontrib>KAWAUCHI, HIROAKI</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>YAKUGAKU ZASSHI</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SUE, HIROSHI</au><au>TAKAYANAGI, GIICHI</au><au>KOSEKI, TOMOKO</au><au>NITTA, KAZUO</au><au>SAKAKIBARA, FUSAO</au><au>KAWAUCHI, HIROAKI</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification, Characterization and Antitumor Activity of Rana nigromaculata Lectin</atitle><jtitle>YAKUGAKU ZASSHI</jtitle><addtitle>YAKUGAKU ZASSHI</addtitle><date>1980-07</date><risdate>1980</risdate><volume>100</volume><issue>7</issue><spage>706</spage><epage>712</epage><pages>706-712</pages><issn>0031-6903</issn><eissn>1347-5231</eissn><abstract>The lectin from Rana nigromaculata eggs was isolated by Sephadex G-75 gel filtration, DEAE-cellulose and Hydroxylapatite column chromatography. Isolated lectin was obtained in a homogeneous state by polyacrylamide gel electrophoresis (PAGE), and characterized as a basic protein with a molecular weight of 15500 by SDS-PAGE and an isoelectric point of pH 9.6 by isoelectric focusing. Amino acid analysis revealed threonine, aspartic acid, serine and qlutamic acid to be the predominant amino acids, the basic amino acids were relatively little. The isolated lectin strongly agglutinated cancer cells from experimental animals. The minimum agglutinating dose of lectin was 2.0 μg/0.2 ml for Ehrlich ascites carcinoma cells and 0.5 μg/0.2 ml for ascites hepatoma 109A cells. Agglutination it was specifically inhibited by ganglioside of human erythrocytes. This lectin strongly inhibited the growth of ascitic Ehrlich carcinoma while it was less active against the solid type.</abstract><cop>Japan</cop><pub>The Pharmaceutical Society of Japan</pub><pmid>7193723</pmid><doi>10.1248/yakushi1947.100.7_706</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0031-6903 |
| ispartof | YAKUGAKU ZASSHI, 1980/07/25, Vol.100(7), pp.706-712 |
| issn | 0031-6903 1347-5231 |
| language | eng ; jpn |
| recordid | cdi_proquest_miscellaneous_75467096 |
| source | MEDLINE; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Alma/SFX Local Collection |
| subjects | Agglutination - drug effects Animals Antineoplastic Agents - isolation & purification antitumor basic protein Chemical Phenomena Chemistry, Physical Female frog eggs ganglioside Humans lectin Lectins - isolation & purification Lectins - pharmacology Male Mice Ovum - analysis rana nigromaculata nigromaculata hallowell Ranidae Rats |
| title | Purification, Characterization and Antitumor Activity of Rana nigromaculata Lectin |
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