Decay accelerating factor of complement is anchored to cells by a C-terminal glycolipid
Membrane-associated decay accelerating factor (DAF) of human erythrocytes (Ehu) was analyzed for a C-terminal glycolipid anchoring structure. Automated amino acid analysis of DAF following reductive radiomethylation revealed ethanolamine and glucosamine residues in proportions identical with those p...
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| Veröffentlicht in: | Biochemistry (Easton) 1986-11, Vol.25 (22), p.6740-6747 |
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| creator | Medof, M. Edward Walter, Elizabeth I Roberts, William L Haas, Robert Rosenberry, Terrone L |
| description | Membrane-associated decay accelerating factor (DAF) of human erythrocytes (Ehu) was analyzed for a C-terminal glycolipid anchoring structure. Automated amino acid analysis of DAF following reductive radiomethylation revealed ethanolamine and glucosamine residues in proportions identical with those present in the Ehu acetylcholinesterase (AChE) anchor. Cleavage of radiomethylated 70-kilodalton (kDa) DAF with papain released the labeled ethanolamine and glucosamine and generated 61- and 55-kDa DAF products that retained all labeled Lys and labeled N-terminal Asp. Incubation of intact Ehu with phosphatidylinositol-specific phospholipase C (PI-PLC), which cleaves the anchors in trypanosome membrane form variant surface glycoproteins (mfVSGs) and murine thymocyte Thy-1 antigen, released 15% of the cell-associated DAF antigen. The released 67-kDa PI-PLC DAF derivative retained its ability to decay the classical C3 convertase C4b2a but was unable to membrane-incorporate and displayed physicochemical properties similar to urine DAF, a hydrophilic DAF form that can be isolated from urine. Nitrous acid deamination cleavage of Ehu DAF at glucosamine following labeling with the lipophilic photoreagent 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine ([125I]TID) released the [125I]TID label in a parallel fashion as from [125I]TID-labeled AChE. Biosynthetic labeling of HeLa cells with [3H]ethanolamine resulted in rapid 3H incorporation into both 48-kDa pro-DAF and 72-kDa mature epithelial cell DAF. Our findings indicate that DAF and AChE are anchored in Ehu by the same or a similar glycolipid structure and that, like VSGs, this structure is incorporated into DAF early in DAF biosynthesis prior to processing of pro-DAF in the Golgi. |
| doi_str_mv | 10.1021/bi00370a003 |
| format | Article |
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Edward ; Walter, Elizabeth I ; Roberts, William L ; Haas, Robert ; Rosenberry, Terrone L</creator><creatorcontrib>Medof, M. Edward ; Walter, Elizabeth I ; Roberts, William L ; Haas, Robert ; Rosenberry, Terrone L ; Case Western Reserve Univ. School of Medicine, Cleveland, OH</creatorcontrib><description>Membrane-associated decay accelerating factor (DAF) of human erythrocytes (Ehu) was analyzed for a C-terminal glycolipid anchoring structure. Automated amino acid analysis of DAF following reductive radiomethylation revealed ethanolamine and glucosamine residues in proportions identical with those present in the Ehu acetylcholinesterase (AChE) anchor. Cleavage of radiomethylated 70-kilodalton (kDa) DAF with papain released the labeled ethanolamine and glucosamine and generated 61- and 55-kDa DAF products that retained all labeled Lys and labeled N-terminal Asp. Incubation of intact Ehu with phosphatidylinositol-specific phospholipase C (PI-PLC), which cleaves the anchors in trypanosome membrane form variant surface glycoproteins (mfVSGs) and murine thymocyte Thy-1 antigen, released 15% of the cell-associated DAF antigen. The released 67-kDa PI-PLC DAF derivative retained its ability to decay the classical C3 convertase C4b2a but was unable to membrane-incorporate and displayed physicochemical properties similar to urine DAF, a hydrophilic DAF form that can be isolated from urine. Nitrous acid deamination cleavage of Ehu DAF at glucosamine following labeling with the lipophilic photoreagent 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine ([125I]TID) released the [125I]TID label in a parallel fashion as from [125I]TID-labeled AChE. Biosynthetic labeling of HeLa cells with [3H]ethanolamine resulted in rapid 3H incorporation into both 48-kDa pro-DAF and 72-kDa mature epithelial cell DAF. Our findings indicate that DAF and AChE are anchored in Ehu by the same or a similar glycolipid structure and that, like VSGs, this structure is incorporated into DAF early in DAF biosynthesis prior to processing of pro-DAF in the Golgi.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00370a003</identifier><identifier>PMID: 2432921</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>550201 - Biochemistry- Tracer Techniques ; AMINES ; AMINO ACID SEQUENCE ; Anemias. Hemoglobinopathies ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; BIOCHEMISTRY ; Biological and medical sciences ; BIOLOGICAL MATERIALS ; BLOOD ; BLOOD CELLS ; BODY FLUIDS ; CARBOHYDRATES ; CARBOXYLESTERASES ; CD55 Antigens ; CELL CONSTITUENTS ; CELL MEMBRANES ; CHEMISTRY ; CHOLINESTERASE ; Chromatography, Affinity ; COMPLEMENT ; Complement Inactivator Proteins - metabolism ; DAYS LIVING RADIOISOTOPES ; Diseases of red blood cells ; ELECTRON CAPTURE RADIOISOTOPES ; ENZYMES ; ERYTHROCYTES ; ESTERASES ; Ethanolamine ; Ethanolamines - analysis ; GLUCOSAMINE ; Glucosamine - analysis ; GLYCOLIPIDS ; Glycolipids - analysis ; HELA CELLS ; HeLa Cells - metabolism ; Hematologic and hematopoietic diseases ; HEXOSAMINES ; HEXOSES ; Humans ; HYDROLASES ; IMMUNOASSAY ; IMMUNOLOGY ; INTERMEDIATE MASS NUCLEI ; IODINE 125 ; IODINE ISOTOPES ; ISOTOPE APPLICATIONS ; ISOTOPES ; Kinetics ; LABELLED COMPOUNDS ; LIPIDS ; man ; MATERIALS ; Medical sciences ; Membrane Proteins - biosynthesis ; Membrane Proteins - isolation & purification ; Membrane Proteins - metabolism ; MEMBRANES ; MOLECULAR STRUCTURE ; MONOSACCHARIDES ; NUCLEI ; ODD-EVEN NUCLEI ; ORGANIC COMPOUNDS ; PEPTIDES ; POLYPEPTIDES ; Protein Binding ; PROTEINS ; RADIOASSAY ; RADIOIMMUNOASSAY ; RADIOIMMUNOLOGY ; RADIOISOTOPES ; SACCHARIDES ; TRACER TECHNIQUES ; TRITIUM COMPOUNDS ; UPTAKE</subject><ispartof>Biochemistry (Easton), 1986-11, Vol.25 (22), p.6740-6747</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a507t-3d246cad2685c86d2c00c5b8598cc05b21f868c866d9992059108518fe2725b73</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00370a003$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00370a003$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,885,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8332820$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2432921$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/6479444$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Medof, M. Edward</creatorcontrib><creatorcontrib>Walter, Elizabeth I</creatorcontrib><creatorcontrib>Roberts, William L</creatorcontrib><creatorcontrib>Haas, Robert</creatorcontrib><creatorcontrib>Rosenberry, Terrone L</creatorcontrib><creatorcontrib>Case Western Reserve Univ. School of Medicine, Cleveland, OH</creatorcontrib><title>Decay accelerating factor of complement is anchored to cells by a C-terminal glycolipid</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Membrane-associated decay accelerating factor (DAF) of human erythrocytes (Ehu) was analyzed for a C-terminal glycolipid anchoring structure. Automated amino acid analysis of DAF following reductive radiomethylation revealed ethanolamine and glucosamine residues in proportions identical with those present in the Ehu acetylcholinesterase (AChE) anchor. Cleavage of radiomethylated 70-kilodalton (kDa) DAF with papain released the labeled ethanolamine and glucosamine and generated 61- and 55-kDa DAF products that retained all labeled Lys and labeled N-terminal Asp. Incubation of intact Ehu with phosphatidylinositol-specific phospholipase C (PI-PLC), which cleaves the anchors in trypanosome membrane form variant surface glycoproteins (mfVSGs) and murine thymocyte Thy-1 antigen, released 15% of the cell-associated DAF antigen. The released 67-kDa PI-PLC DAF derivative retained its ability to decay the classical C3 convertase C4b2a but was unable to membrane-incorporate and displayed physicochemical properties similar to urine DAF, a hydrophilic DAF form that can be isolated from urine. Nitrous acid deamination cleavage of Ehu DAF at glucosamine following labeling with the lipophilic photoreagent 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine ([125I]TID) released the [125I]TID label in a parallel fashion as from [125I]TID-labeled AChE. Biosynthetic labeling of HeLa cells with [3H]ethanolamine resulted in rapid 3H incorporation into both 48-kDa pro-DAF and 72-kDa mature epithelial cell DAF. Our findings indicate that DAF and AChE are anchored in Ehu by the same or a similar glycolipid structure and that, like VSGs, this structure is incorporated into DAF early in DAF biosynthesis prior to processing of pro-DAF in the Golgi.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>AMINES</subject><subject>AMINO ACID SEQUENCE</subject><subject>Anemias. Hemoglobinopathies</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BIOCHEMISTRY</subject><subject>Biological and medical sciences</subject><subject>BIOLOGICAL MATERIALS</subject><subject>BLOOD</subject><subject>BLOOD CELLS</subject><subject>BODY FLUIDS</subject><subject>CARBOHYDRATES</subject><subject>CARBOXYLESTERASES</subject><subject>CD55 Antigens</subject><subject>CELL CONSTITUENTS</subject><subject>CELL MEMBRANES</subject><subject>CHEMISTRY</subject><subject>CHOLINESTERASE</subject><subject>Chromatography, Affinity</subject><subject>COMPLEMENT</subject><subject>Complement Inactivator Proteins - metabolism</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>Diseases of red blood cells</subject><subject>ELECTRON CAPTURE RADIOISOTOPES</subject><subject>ENZYMES</subject><subject>ERYTHROCYTES</subject><subject>ESTERASES</subject><subject>Ethanolamine</subject><subject>Ethanolamines - analysis</subject><subject>GLUCOSAMINE</subject><subject>Glucosamine - analysis</subject><subject>GLYCOLIPIDS</subject><subject>Glycolipids - analysis</subject><subject>HELA CELLS</subject><subject>HeLa Cells - metabolism</subject><subject>Hematologic and hematopoietic diseases</subject><subject>HEXOSAMINES</subject><subject>HEXOSES</subject><subject>Humans</subject><subject>HYDROLASES</subject><subject>IMMUNOASSAY</subject><subject>IMMUNOLOGY</subject><subject>INTERMEDIATE MASS NUCLEI</subject><subject>IODINE 125</subject><subject>IODINE ISOTOPES</subject><subject>ISOTOPE APPLICATIONS</subject><subject>ISOTOPES</subject><subject>Kinetics</subject><subject>LABELLED COMPOUNDS</subject><subject>LIPIDS</subject><subject>man</subject><subject>MATERIALS</subject><subject>Medical sciences</subject><subject>Membrane Proteins - biosynthesis</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>MEMBRANES</subject><subject>MOLECULAR STRUCTURE</subject><subject>MONOSACCHARIDES</subject><subject>NUCLEI</subject><subject>ODD-EVEN NUCLEI</subject><subject>ORGANIC COMPOUNDS</subject><subject>PEPTIDES</subject><subject>POLYPEPTIDES</subject><subject>Protein Binding</subject><subject>PROTEINS</subject><subject>RADIOASSAY</subject><subject>RADIOIMMUNOASSAY</subject><subject>RADIOIMMUNOLOGY</subject><subject>RADIOISOTOPES</subject><subject>SACCHARIDES</subject><subject>TRACER TECHNIQUES</subject><subject>TRITIUM COMPOUNDS</subject><subject>UPTAKE</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9rFDEUB_AgSt1WT56FIKIHGU0y-XmsW6tC_QGt6C1k3mTa1JnJmmTB_e9NmWXxIHhJCN9PHsl7CD2h5DUljL7pAiGtIq6u99CKCkYaboy4j1aEENkwI8lDdJzzbT1yovgROmK8ZYbRFfp-5sHtsAPwo0-uhPkaDw5KTDgOGOK0Gf3k54JDxm6Gm5h8j0vElY8Zd_UmXjfFpynMbsTX4w7iGDahf4QeDG7M_vF-P0Hfzt9drT80F1_ef1yfXjROEFWatmdcguuZ1AK07BkQAqLTwmgAIjpGBy11TWRvjGFEGEq0oHrwTDHRqfYEPVvqxlyCzRCKhxuI8-yhWMmV4ZxX9GJBmxR_bX0udgr57gdu9nGbrVK1H0rK_0LKhVS6NRW-WiCkmHPyg92kMLm0s5TYu6HYv4ZS9dN92W03-f5g91Oo-fN97jK4cUi10yEfmG5bphmprFlYyMX_PsQu_bRStUrYq6-X9sf5J_NWfV7by-pfLt5Btrdxm-qI8j8f-AfTEqzJ</recordid><startdate>19861104</startdate><enddate>19861104</enddate><creator>Medof, M. Edward</creator><creator>Walter, Elizabeth I</creator><creator>Roberts, William L</creator><creator>Haas, Robert</creator><creator>Rosenberry, Terrone L</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>7T5</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19861104</creationdate><title>Decay accelerating factor of complement is anchored to cells by a C-terminal glycolipid</title><author>Medof, M. Edward ; Walter, Elizabeth I ; Roberts, William L ; Haas, Robert ; Rosenberry, Terrone L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a507t-3d246cad2685c86d2c00c5b8598cc05b21f868c866d9992059108518fe2725b73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>AMINES</topic><topic>AMINO ACID SEQUENCE</topic><topic>Anemias. Hemoglobinopathies</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BIOCHEMISTRY</topic><topic>Biological and medical sciences</topic><topic>BIOLOGICAL MATERIALS</topic><topic>BLOOD</topic><topic>BLOOD CELLS</topic><topic>BODY FLUIDS</topic><topic>CARBOHYDRATES</topic><topic>CARBOXYLESTERASES</topic><topic>CD55 Antigens</topic><topic>CELL CONSTITUENTS</topic><topic>CELL MEMBRANES</topic><topic>CHEMISTRY</topic><topic>CHOLINESTERASE</topic><topic>Chromatography, Affinity</topic><topic>COMPLEMENT</topic><topic>Complement Inactivator Proteins - metabolism</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>Diseases of red blood cells</topic><topic>ELECTRON CAPTURE RADIOISOTOPES</topic><topic>ENZYMES</topic><topic>ERYTHROCYTES</topic><topic>ESTERASES</topic><topic>Ethanolamine</topic><topic>Ethanolamines - analysis</topic><topic>GLUCOSAMINE</topic><topic>Glucosamine - analysis</topic><topic>GLYCOLIPIDS</topic><topic>Glycolipids - analysis</topic><topic>HELA CELLS</topic><topic>HeLa Cells - metabolism</topic><topic>Hematologic and hematopoietic diseases</topic><topic>HEXOSAMINES</topic><topic>HEXOSES</topic><topic>Humans</topic><topic>HYDROLASES</topic><topic>IMMUNOASSAY</topic><topic>IMMUNOLOGY</topic><topic>INTERMEDIATE MASS NUCLEI</topic><topic>IODINE 125</topic><topic>IODINE ISOTOPES</topic><topic>ISOTOPE APPLICATIONS</topic><topic>ISOTOPES</topic><topic>Kinetics</topic><topic>LABELLED COMPOUNDS</topic><topic>LIPIDS</topic><topic>man</topic><topic>MATERIALS</topic><topic>Medical sciences</topic><topic>Membrane Proteins - biosynthesis</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Membrane Proteins - metabolism</topic><topic>MEMBRANES</topic><topic>MOLECULAR STRUCTURE</topic><topic>MONOSACCHARIDES</topic><topic>NUCLEI</topic><topic>ODD-EVEN NUCLEI</topic><topic>ORGANIC COMPOUNDS</topic><topic>PEPTIDES</topic><topic>POLYPEPTIDES</topic><topic>Protein Binding</topic><topic>PROTEINS</topic><topic>RADIOASSAY</topic><topic>RADIOIMMUNOASSAY</topic><topic>RADIOIMMUNOLOGY</topic><topic>RADIOISOTOPES</topic><topic>SACCHARIDES</topic><topic>TRACER TECHNIQUES</topic><topic>TRITIUM COMPOUNDS</topic><topic>UPTAKE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Medof, M. Edward</creatorcontrib><creatorcontrib>Walter, Elizabeth I</creatorcontrib><creatorcontrib>Roberts, William L</creatorcontrib><creatorcontrib>Haas, Robert</creatorcontrib><creatorcontrib>Rosenberry, Terrone L</creatorcontrib><creatorcontrib>Case Western Reserve Univ. School of Medicine, Cleveland, OH</creatorcontrib><collection>Istex</collection><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>Immunology Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Medof, M. Edward</au><au>Walter, Elizabeth I</au><au>Roberts, William L</au><au>Haas, Robert</au><au>Rosenberry, Terrone L</au><aucorp>Case Western Reserve Univ. School of Medicine, Cleveland, OH</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Decay accelerating factor of complement is anchored to cells by a C-terminal glycolipid</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1986-11-04</date><risdate>1986</risdate><volume>25</volume><issue>22</issue><spage>6740</spage><epage>6747</epage><pages>6740-6747</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Membrane-associated decay accelerating factor (DAF) of human erythrocytes (Ehu) was analyzed for a C-terminal glycolipid anchoring structure. Automated amino acid analysis of DAF following reductive radiomethylation revealed ethanolamine and glucosamine residues in proportions identical with those present in the Ehu acetylcholinesterase (AChE) anchor. Cleavage of radiomethylated 70-kilodalton (kDa) DAF with papain released the labeled ethanolamine and glucosamine and generated 61- and 55-kDa DAF products that retained all labeled Lys and labeled N-terminal Asp. Incubation of intact Ehu with phosphatidylinositol-specific phospholipase C (PI-PLC), which cleaves the anchors in trypanosome membrane form variant surface glycoproteins (mfVSGs) and murine thymocyte Thy-1 antigen, released 15% of the cell-associated DAF antigen. The released 67-kDa PI-PLC DAF derivative retained its ability to decay the classical C3 convertase C4b2a but was unable to membrane-incorporate and displayed physicochemical properties similar to urine DAF, a hydrophilic DAF form that can be isolated from urine. Nitrous acid deamination cleavage of Ehu DAF at glucosamine following labeling with the lipophilic photoreagent 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine ([125I]TID) released the [125I]TID label in a parallel fashion as from [125I]TID-labeled AChE. Biosynthetic labeling of HeLa cells with [3H]ethanolamine resulted in rapid 3H incorporation into both 48-kDa pro-DAF and 72-kDa mature epithelial cell DAF. Our findings indicate that DAF and AChE are anchored in Ehu by the same or a similar glycolipid structure and that, like VSGs, this structure is incorporated into DAF early in DAF biosynthesis prior to processing of pro-DAF in the Golgi.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>2432921</pmid><doi>10.1021/bi00370a003</doi><tpages>8</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 1986-11, Vol.25 (22), p.6740-6747 |
| issn | 0006-2960 1520-4995 |
| language | eng |
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| source | MEDLINE; ACS Publications |
| subjects | 550201 - Biochemistry- Tracer Techniques AMINES AMINO ACID SEQUENCE Anemias. Hemoglobinopathies BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES BIOCHEMISTRY Biological and medical sciences BIOLOGICAL MATERIALS BLOOD BLOOD CELLS BODY FLUIDS CARBOHYDRATES CARBOXYLESTERASES CD55 Antigens CELL CONSTITUENTS CELL MEMBRANES CHEMISTRY CHOLINESTERASE Chromatography, Affinity COMPLEMENT Complement Inactivator Proteins - metabolism DAYS LIVING RADIOISOTOPES Diseases of red blood cells ELECTRON CAPTURE RADIOISOTOPES ENZYMES ERYTHROCYTES ESTERASES Ethanolamine Ethanolamines - analysis GLUCOSAMINE Glucosamine - analysis GLYCOLIPIDS Glycolipids - analysis HELA CELLS HeLa Cells - metabolism Hematologic and hematopoietic diseases HEXOSAMINES HEXOSES Humans HYDROLASES IMMUNOASSAY IMMUNOLOGY INTERMEDIATE MASS NUCLEI IODINE 125 IODINE ISOTOPES ISOTOPE APPLICATIONS ISOTOPES Kinetics LABELLED COMPOUNDS LIPIDS man MATERIALS Medical sciences Membrane Proteins - biosynthesis Membrane Proteins - isolation & purification Membrane Proteins - metabolism MEMBRANES MOLECULAR STRUCTURE MONOSACCHARIDES NUCLEI ODD-EVEN NUCLEI ORGANIC COMPOUNDS PEPTIDES POLYPEPTIDES Protein Binding PROTEINS RADIOASSAY RADIOIMMUNOASSAY RADIOIMMUNOLOGY RADIOISOTOPES SACCHARIDES TRACER TECHNIQUES TRITIUM COMPOUNDS UPTAKE |
| title | Decay accelerating factor of complement is anchored to cells by a C-terminal glycolipid |
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