A mammalian sperm lectin related to rat hepatocyte lectin-2/3 : purification from rabbit testis and identification as a zona binding protein
In rat liver the asialoglycoprotein receptor is composed of three polypeptides, RHL-1, RHL-2 and RHL-3. In rat testis and spermatozoa a galactosyl receptor (RTG-r) which is immunologically related to RHL-2/3 has been described. We now report that in addition to its presence in the rat, an antigenic...
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Veröffentlicht in: | Molecular and cellular biochemistry 1991-05, Vol.103 (2), p.155-161 |
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description | In rat liver the asialoglycoprotein receptor is composed of three polypeptides, RHL-1, RHL-2 and RHL-3. In rat testis and spermatozoa a galactosyl receptor (RTG-r) which is immunologically related to RHL-2/3 has been described. We now report that in addition to its presence in the rat, an antigenic species of 54 kDa related to RHL-2/3 is present on rabbit, human, pig and mouse spermatozoa. Purified rabbit testis galactosyl receptor (RbTG-r) consists of two major proteins of 54 and 49 kDa, while purified rabbit liver galactose lectin consists of two major proteins of 43 and 40 kDa. In an ELISA the purified rabbit testis galactosyl receptor was shown to bind biotinylated heat solubilized rabbit zonae, while the purified liver galactose lectin did not. We conclude that one of the mammalian sperm's zona binding proteins is a galactose lectin of 54 kDa related to rat liver RHL-2/3. |
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E ; O'RAND, M. G</creator><creatorcontrib>MUNIR ABDULLAH ; WIDGREN, E. E ; O'RAND, M. G</creatorcontrib><description>In rat liver the asialoglycoprotein receptor is composed of three polypeptides, RHL-1, RHL-2 and RHL-3. In rat testis and spermatozoa a galactosyl receptor (RTG-r) which is immunologically related to RHL-2/3 has been described. We now report that in addition to its presence in the rat, an antigenic species of 54 kDa related to RHL-2/3 is present on rabbit, human, pig and mouse spermatozoa. Purified rabbit testis galactosyl receptor (RbTG-r) consists of two major proteins of 54 and 49 kDa, while purified rabbit liver galactose lectin consists of two major proteins of 43 and 40 kDa. In an ELISA the purified rabbit testis galactosyl receptor was shown to bind biotinylated heat solubilized rabbit zonae, while the purified liver galactose lectin did not. We conclude that one of the mammalian sperm's zona binding proteins is a galactose lectin of 54 kDa related to rat liver RHL-2/3.</description><identifier>ISSN: 0300-8177</identifier><identifier>EISSN: 1573-4919</identifier><identifier>DOI: 10.1007/BF00227482</identifier><identifier>PMID: 1712896</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Asialoglycoprotein Receptor ; Biological and medical sciences ; Blotting, Western ; Cross Reactions ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; Humans ; Immunoenzyme Techniques ; Lectins - analysis ; Lectins - immunology ; Lectins - isolation & purification ; Lectins - metabolism ; Liver - chemistry ; Male ; Mice ; Proteins ; Rabbits ; Rats ; Receptors, Cell Surface - analysis ; Receptors, Cell Surface - immunology ; Receptors, Cell Surface - isolation & purification ; Receptors, Cell Surface - metabolism ; Receptors, Immunologic - chemistry ; Receptors, Immunologic - immunology ; spermatozoa ; Spermatozoa - chemistry ; Spermatozoa - immunology ; Staining and Labeling ; Testis - chemistry ; Testis - immunology ; Zona Pellucida - metabolism ; zona-binding protein</subject><ispartof>Molecular and cellular biochemistry, 1991-05, Vol.103 (2), p.155-161</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27902,27903</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19819542$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1712896$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MUNIR ABDULLAH</creatorcontrib><creatorcontrib>WIDGREN, E. E</creatorcontrib><creatorcontrib>O'RAND, M. G</creatorcontrib><title>A mammalian sperm lectin related to rat hepatocyte lectin-2/3 : purification from rabbit testis and identification as a zona binding protein</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><description>In rat liver the asialoglycoprotein receptor is composed of three polypeptides, RHL-1, RHL-2 and RHL-3. In rat testis and spermatozoa a galactosyl receptor (RTG-r) which is immunologically related to RHL-2/3 has been described. We now report that in addition to its presence in the rat, an antigenic species of 54 kDa related to RHL-2/3 is present on rabbit, human, pig and mouse spermatozoa. Purified rabbit testis galactosyl receptor (RbTG-r) consists of two major proteins of 54 and 49 kDa, while purified rabbit liver galactose lectin consists of two major proteins of 43 and 40 kDa. In an ELISA the purified rabbit testis galactosyl receptor was shown to bind biotinylated heat solubilized rabbit zonae, while the purified liver galactose lectin did not. We conclude that one of the mammalian sperm's zona binding proteins is a galactose lectin of 54 kDa related to rat liver RHL-2/3.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Asialoglycoprotein Receptor</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Cross Reactions</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>Humans</subject><subject>Immunoenzyme Techniques</subject><subject>Lectins - analysis</subject><subject>Lectins - immunology</subject><subject>Lectins - isolation & purification</subject><subject>Lectins - metabolism</subject><subject>Liver - chemistry</subject><subject>Male</subject><subject>Mice</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Receptors, Cell Surface - analysis</subject><subject>Receptors, Cell Surface - immunology</subject><subject>Receptors, Cell Surface - isolation & purification</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Immunologic - chemistry</subject><subject>Receptors, Immunologic - immunology</subject><subject>spermatozoa</subject><subject>Spermatozoa - chemistry</subject><subject>Spermatozoa - immunology</subject><subject>Staining and Labeling</subject><subject>Testis - chemistry</subject><subject>Testis - immunology</subject><subject>Zona Pellucida - metabolism</subject><subject>zona-binding protein</subject><issn>0300-8177</issn><issn>1573-4919</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9rFTEQB_AgSn1WL96FXPQgbJtks_nhrS1WCwUv9bxMshON7GbXJO_Q_g3-0Ubeg3f0FJj5MJPhS8hbzi44Y_ry-pYxIbQ04hnZ8UH3nbTcPic71jPWGa71S_KqlF-MNc75GTnjmgtj1Y78uaILLAvMERItG-aFzuhrTDTjDBUnWleaodKfuEFd_WPFI-jEZU8_0W2fY4gealwTDXldmnYuVlqx1FgopInGCVM9KWhV-rQmoC6mKaYfdMtrxZhekxcB5oJvju85-X77-eHma3f_7cvdzdV953smahcGtEqK4JRoR1htnRq4x-CddMb3EwepwuR6YZ1GdHJwOEjjHVrN0HDZn5MPh7lt7-99--e4xOJxniHhui-jYcooI_4PuWJcKaka_HiAPq-lZAzjluMC-XHkbPyX0XjKqOF3x6l7t-B0oodQWv_9sQ_FwxwyJB_LiVnD7SBF_xfu7Jor</recordid><startdate>19910515</startdate><enddate>19910515</enddate><creator>MUNIR ABDULLAH</creator><creator>WIDGREN, E. 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G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c302t-f5e9642fb62289979b651cefcb4b8c3d1a46fdb329b7eeb45be548cbe970e8143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Asialoglycoprotein Receptor</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Cross Reactions</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>Humans</topic><topic>Immunoenzyme Techniques</topic><topic>Lectins - analysis</topic><topic>Lectins - immunology</topic><topic>Lectins - isolation & purification</topic><topic>Lectins - metabolism</topic><topic>Liver - chemistry</topic><topic>Male</topic><topic>Mice</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Receptors, Cell Surface - analysis</topic><topic>Receptors, Cell Surface - immunology</topic><topic>Receptors, Cell Surface - isolation & purification</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Immunologic - chemistry</topic><topic>Receptors, Immunologic - immunology</topic><topic>spermatozoa</topic><topic>Spermatozoa - chemistry</topic><topic>Spermatozoa - immunology</topic><topic>Staining and Labeling</topic><topic>Testis - chemistry</topic><topic>Testis - immunology</topic><topic>Zona Pellucida - metabolism</topic><topic>zona-binding protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MUNIR ABDULLAH</creatorcontrib><creatorcontrib>WIDGREN, E. E</creatorcontrib><creatorcontrib>O'RAND, M. G</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MUNIR ABDULLAH</au><au>WIDGREN, E. E</au><au>O'RAND, M. G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A mammalian sperm lectin related to rat hepatocyte lectin-2/3 : purification from rabbit testis and identification as a zona binding protein</atitle><jtitle>Molecular and cellular biochemistry</jtitle><addtitle>Mol Cell Biochem</addtitle><date>1991-05-15</date><risdate>1991</risdate><volume>103</volume><issue>2</issue><spage>155</spage><epage>161</epage><pages>155-161</pages><issn>0300-8177</issn><eissn>1573-4919</eissn><abstract>In rat liver the asialoglycoprotein receptor is composed of three polypeptides, RHL-1, RHL-2 and RHL-3. In rat testis and spermatozoa a galactosyl receptor (RTG-r) which is immunologically related to RHL-2/3 has been described. We now report that in addition to its presence in the rat, an antigenic species of 54 kDa related to RHL-2/3 is present on rabbit, human, pig and mouse spermatozoa. Purified rabbit testis galactosyl receptor (RbTG-r) consists of two major proteins of 54 and 49 kDa, while purified rabbit liver galactose lectin consists of two major proteins of 43 and 40 kDa. In an ELISA the purified rabbit testis galactosyl receptor was shown to bind biotinylated heat solubilized rabbit zonae, while the purified liver galactose lectin did not. We conclude that one of the mammalian sperm's zona binding proteins is a galactose lectin of 54 kDa related to rat liver RHL-2/3.</abstract><cop>Dordrecht</cop><pub>Springer</pub><pmid>1712896</pmid><doi>10.1007/BF00227482</doi><tpages>7</tpages></addata></record> |
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subjects | Analytical, structural and metabolic biochemistry Animals Asialoglycoprotein Receptor Biological and medical sciences Blotting, Western Cross Reactions Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Glycoproteins Humans Immunoenzyme Techniques Lectins - analysis Lectins - immunology Lectins - isolation & purification Lectins - metabolism Liver - chemistry Male Mice Proteins Rabbits Rats Receptors, Cell Surface - analysis Receptors, Cell Surface - immunology Receptors, Cell Surface - isolation & purification Receptors, Cell Surface - metabolism Receptors, Immunologic - chemistry Receptors, Immunologic - immunology spermatozoa Spermatozoa - chemistry Spermatozoa - immunology Staining and Labeling Testis - chemistry Testis - immunology Zona Pellucida - metabolism zona-binding protein |
title | A mammalian sperm lectin related to rat hepatocyte lectin-2/3 : purification from rabbit testis and identification as a zona binding protein |
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