Identification and isolation of the Leishmania transferrin receptor
In a previous report, we have presented several lines of evidence, derived from widely different methodologies, suggesting that Leishmania has specific receptors for transferrin with a Kd similar to the mammalian transferrin receptor. This paper describes the identification, purification, and bioche...
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Veröffentlicht in: | The Journal of biological chemistry 1992-05, Vol.267 (13), p.9112-9117 |
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creator | VOYIATZAKI, C. S SOTERIADOU, K. P |
description | In a previous report, we have presented several lines of evidence, derived from widely different methodologies, suggesting
that Leishmania has specific receptors for transferrin with a Kd similar to the mammalian transferrin receptor. This paper
describes the identification, purification, and biochemical characterization of Leishmania transferrin receptor. The Leishmania
transferrin receptor, detected on intact parasites by immunoperoxidase staining, was first identified by sodium dodecyl sulfate-polyacrylamide
gel electrophoresis followed by Western blot analysis, using 125I-transferrin, as a 70-kDa protein. It has been isolated initially
from Leishmania infantum promastigotes using affinity chromatography on a transferrin-Sepharose column and, subsequently,
from Leishmania major promastigotes. The use of polyclonal antisera to the purified 70-kDa Leishmania transferrin receptor
and to the purified rat transferrin receptor showed that the two receptors are antigenically distinct. The 70-kDa Leishmania
transferrin receptor was subsequently characterized as an integral membrane glycoprotein. The monomeric state of the Leishmania
transferrin receptor was demonstrated by gel filtration of purified receptor complexed with 125I-transferrin. Thus, the Leishmania
transferrin receptor, unlike the mammalian receptor, is not a disulfide-linked dimer but a single 70-kDa polypeptide. |
doi_str_mv | 10.1016/s0021-9258(19)50396-9 |
format | Article |
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that Leishmania has specific receptors for transferrin with a Kd similar to the mammalian transferrin receptor. This paper
describes the identification, purification, and biochemical characterization of Leishmania transferrin receptor. The Leishmania
transferrin receptor, detected on intact parasites by immunoperoxidase staining, was first identified by sodium dodecyl sulfate-polyacrylamide
gel electrophoresis followed by Western blot analysis, using 125I-transferrin, as a 70-kDa protein. It has been isolated initially
from Leishmania infantum promastigotes using affinity chromatography on a transferrin-Sepharose column and, subsequently,
from Leishmania major promastigotes. The use of polyclonal antisera to the purified 70-kDa Leishmania transferrin receptor
and to the purified rat transferrin receptor showed that the two receptors are antigenically distinct. The 70-kDa Leishmania
transferrin receptor was subsequently characterized as an integral membrane glycoprotein. The monomeric state of the Leishmania
transferrin receptor was demonstrated by gel filtration of purified receptor complexed with 125I-transferrin. Thus, the Leishmania
transferrin receptor, unlike the mammalian receptor, is not a disulfide-linked dimer but a single 70-kDa polypeptide.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(19)50396-9</identifier><identifier>PMID: 1577747</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Biological and medical sciences ; Blotting, Western ; Cell receptors ; Cell structures and functions ; Chromatography, Gel ; Cross-Linking Reagents ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Humans ; identification ; Immunoenzyme Techniques ; isolation ; Leishmania ; Leishmania - chemistry ; Leishmania donovani - chemistry ; membrane proteins ; Miscellaneous ; Molecular and cellular biology ; Radioimmunoassay ; Rats ; receptors ; Receptors, Transferrin - isolation & purification ; transferrin</subject><ispartof>The Journal of biological chemistry, 1992-05, Vol.267 (13), p.9112-9117</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c505t-c0b5b7e4b242d374effd046a3929cae0145349ca4284aaa7e0bb6d423681e88d3</citedby><cites>FETCH-LOGICAL-c505t-c0b5b7e4b242d374effd046a3929cae0145349ca4284aaa7e0bb6d423681e88d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5309635$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1577747$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>VOYIATZAKI, C. S</creatorcontrib><creatorcontrib>SOTERIADOU, K. P</creatorcontrib><title>Identification and isolation of the Leishmania transferrin receptor</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>In a previous report, we have presented several lines of evidence, derived from widely different methodologies, suggesting
that Leishmania has specific receptors for transferrin with a Kd similar to the mammalian transferrin receptor. This paper
describes the identification, purification, and biochemical characterization of Leishmania transferrin receptor. The Leishmania
transferrin receptor, detected on intact parasites by immunoperoxidase staining, was first identified by sodium dodecyl sulfate-polyacrylamide
gel electrophoresis followed by Western blot analysis, using 125I-transferrin, as a 70-kDa protein. It has been isolated initially
from Leishmania infantum promastigotes using affinity chromatography on a transferrin-Sepharose column and, subsequently,
from Leishmania major promastigotes. The use of polyclonal antisera to the purified 70-kDa Leishmania transferrin receptor
and to the purified rat transferrin receptor showed that the two receptors are antigenically distinct. The 70-kDa Leishmania
transferrin receptor was subsequently characterized as an integral membrane glycoprotein. The monomeric state of the Leishmania
transferrin receptor was demonstrated by gel filtration of purified receptor complexed with 125I-transferrin. Thus, the Leishmania
transferrin receptor, unlike the mammalian receptor, is not a disulfide-linked dimer but a single 70-kDa polypeptide.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Chromatography, Gel</subject><subject>Cross-Linking Reagents</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>identification</subject><subject>Immunoenzyme Techniques</subject><subject>isolation</subject><subject>Leishmania</subject><subject>Leishmania - chemistry</subject><subject>Leishmania donovani - chemistry</subject><subject>membrane proteins</subject><subject>Miscellaneous</subject><subject>Molecular and cellular biology</subject><subject>Radioimmunoassay</subject><subject>Rats</subject><subject>receptors</subject><subject>Receptors, Transferrin - isolation & purification</subject><subject>transferrin</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtr20AQgJfQ4LpOfoJB0BLag5qdfWqPwfRhMOSQBHJbVqtRtUUPZ1cm5N9Xjkxy7FxmhvlmBj5C1kC_AwV1nShlkBsmi69gvknKjcrNGVkCLXjOJTx-IMs35CP5lNJfOoUwsCALkFproZdks62wH0MdvBvD0Geur7KQhnbuhjobG8x2GFLTuT64bIyuTzXGGPososf9OMQLcl67NuHlKa_Iw88f95vf-e7213Zzs8u9pHLMPS1lqVGUTLCKa4F1XVGhHDfMeIcUhORiqgQrhHNOIy1LVQnGVQFYFBVfkav57j4OTwdMo-1C8ti2rsfhkKxmhikh9X9BUKCNFmIC5Qz6OKQUsbb7GDoXXyxQe7Rs744K7VGhBWNfLVsz7a1PDw5lh9X71qx1mn85zV3yrq0naT6kN0xyahSXE_Z5xprwp3kOEW0ZBt9gZ5nSFrg1AIz_A2T_kF4</recordid><startdate>19920505</startdate><enddate>19920505</enddate><creator>VOYIATZAKI, C. S</creator><creator>SOTERIADOU, K. P</creator><general>American Society for Biochemistry and Molecular Biology</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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920505</creationdate><title>Identification and isolation of the Leishmania transferrin receptor</title><author>VOYIATZAKI, C. S ; SOTERIADOU, K. P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-c0b5b7e4b242d374effd046a3929cae0145349ca4284aaa7e0bb6d423681e88d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Chromatography, Gel</topic><topic>Cross-Linking Reagents</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>identification</topic><topic>Immunoenzyme Techniques</topic><topic>isolation</topic><topic>Leishmania</topic><topic>Leishmania - chemistry</topic><topic>Leishmania donovani - chemistry</topic><topic>membrane proteins</topic><topic>Miscellaneous</topic><topic>Molecular and cellular biology</topic><topic>Radioimmunoassay</topic><topic>Rats</topic><topic>receptors</topic><topic>Receptors, Transferrin - isolation & purification</topic><topic>transferrin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>VOYIATZAKI, C. S</creatorcontrib><creatorcontrib>SOTERIADOU, K. P</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>VOYIATZAKI, C. S</au><au>SOTERIADOU, K. P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and isolation of the Leishmania transferrin receptor</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-05-05</date><risdate>1992</risdate><volume>267</volume><issue>13</issue><spage>9112</spage><epage>9117</epage><pages>9112-9117</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>In a previous report, we have presented several lines of evidence, derived from widely different methodologies, suggesting
that Leishmania has specific receptors for transferrin with a Kd similar to the mammalian transferrin receptor. This paper
describes the identification, purification, and biochemical characterization of Leishmania transferrin receptor. The Leishmania
transferrin receptor, detected on intact parasites by immunoperoxidase staining, was first identified by sodium dodecyl sulfate-polyacrylamide
gel electrophoresis followed by Western blot analysis, using 125I-transferrin, as a 70-kDa protein. It has been isolated initially
from Leishmania infantum promastigotes using affinity chromatography on a transferrin-Sepharose column and, subsequently,
from Leishmania major promastigotes. The use of polyclonal antisera to the purified 70-kDa Leishmania transferrin receptor
and to the purified rat transferrin receptor showed that the two receptors are antigenically distinct. The 70-kDa Leishmania
transferrin receptor was subsequently characterized as an integral membrane glycoprotein. The monomeric state of the Leishmania
transferrin receptor was demonstrated by gel filtration of purified receptor complexed with 125I-transferrin. Thus, the Leishmania
transferrin receptor, unlike the mammalian receptor, is not a disulfide-linked dimer but a single 70-kDa polypeptide.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1577747</pmid><doi>10.1016/s0021-9258(19)50396-9</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
subjects | Animals Biological and medical sciences Blotting, Western Cell receptors Cell structures and functions Chromatography, Gel Cross-Linking Reagents Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Humans identification Immunoenzyme Techniques isolation Leishmania Leishmania - chemistry Leishmania donovani - chemistry membrane proteins Miscellaneous Molecular and cellular biology Radioimmunoassay Rats receptors Receptors, Transferrin - isolation & purification transferrin |
title | Identification and isolation of the Leishmania transferrin receptor |
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