Isolation and characterization of the glycosaminoglycan component of rabbit thrombomodulin proteoglycan
Previous studies on rabbit thrombomodulin (TM) revealed that certain anticoagulant activities expressed by TM depend on the presence of an acidic domain tentatively identified as a sulfated galactosaminoglycan (Bourin, M.-C., Ohlin, A.-K., Lane, D., Stenflo, J., and Lindahl, U. (1988) J. Biol. Chem....
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| Veröffentlicht in: | The Journal of biological chemistry 1990-09, Vol.265 (26), p.15424-15431 |
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| creator | Bourin, M-C Lundgren-Aakerlund, E Lindahl, U |
| description | Previous studies on rabbit thrombomodulin (TM) revealed that certain anticoagulant activities expressed by TM depend on the
presence of an acidic domain tentatively identified as a sulfated galactosaminoglycan (Bourin, M.-C., Ohlin, A.-K., Lane,
D., Stenflo, J., and Lindahl, U. (1988) J. Biol. Chem. 263, 8044-8052). The glycan was released by alkaline beta-elimination,
isolated by ion-exchange chromatography, and radiolabeled by partial N-deacetylation (hydrazinolysis) followed by re-N-[3H]acetylation.
The labeled product behaved like standard chondroitin sulfate on ion-exchange chromatography, exhibited a Mr of 10-12 x 10(3)
on gel chromatography, and was susceptible to degradation by chondroitinase and testicular hyaluronidase. The major labeled
degradation products following digestion of the glycosaminoglycan with chondroitinase were identified, depending on the incubation
conditions, either as 4/6-mono-O-sulfated, 4,5-unsaturated disaccharides (delta HexA-GalNAc(S] and N-acetylgalactosamine 4,6-di-O-sulfate
(GalcNAc (diS], the latter component accounting for approximately 25% of the total label, or as a major fraction of labeled
trisaccharide, with the predominant structure GalNAc(diS)-GlcA-GalNAc(diS). The terminal GalNAc(diS) unit (not substituted
at C3) was shown to be more susceptible to N-deacetylation during hydrazinolysis than were the internal GalNAc units (substituted
at C3), and thus was more extensively labeled, resulting in over-representation of this unit. It is concluded that rabbit
TM is a chondroitin sulfate proteoglycan, which carries a single glycan side chain characterized by an unusual accumulation
of sulfate groups at the nonreducing terminus. Metabolically 35S-labeled TM was isolated from cultured rabbit heart endothelial
cells and characterized as a chondroitin sulfate proteoglycan which accounted for 1-2% of the total 35S-labeled cell-associated
macromolecules. The isolated chondroitin sulfate showed weaker antithrombin-dependent anticoagulant activity, on a molar basis,
than the intact TM proteoglycan. The anticoagulant action of TM thus depends on a unique form of functional collaboration
between the different constituents of a glycoconjugate. |
| doi_str_mv | 10.1016/S0021-9258(18)55414-4 |
| format | Article |
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presence of an acidic domain tentatively identified as a sulfated galactosaminoglycan (Bourin, M.-C., Ohlin, A.-K., Lane,
D., Stenflo, J., and Lindahl, U. (1988) J. Biol. Chem. 263, 8044-8052). The glycan was released by alkaline beta-elimination,
isolated by ion-exchange chromatography, and radiolabeled by partial N-deacetylation (hydrazinolysis) followed by re-N-[3H]acetylation.
The labeled product behaved like standard chondroitin sulfate on ion-exchange chromatography, exhibited a Mr of 10-12 x 10(3)
on gel chromatography, and was susceptible to degradation by chondroitinase and testicular hyaluronidase. The major labeled
degradation products following digestion of the glycosaminoglycan with chondroitinase were identified, depending on the incubation
conditions, either as 4/6-mono-O-sulfated, 4,5-unsaturated disaccharides (delta HexA-GalNAc(S] and N-acetylgalactosamine 4,6-di-O-sulfate
(GalcNAc (diS], the latter component accounting for approximately 25% of the total label, or as a major fraction of labeled
trisaccharide, with the predominant structure GalNAc(diS)-GlcA-GalNAc(diS). The terminal GalNAc(diS) unit (not substituted
at C3) was shown to be more susceptible to N-deacetylation during hydrazinolysis than were the internal GalNAc units (substituted
at C3), and thus was more extensively labeled, resulting in over-representation of this unit. It is concluded that rabbit
TM is a chondroitin sulfate proteoglycan, which carries a single glycan side chain characterized by an unusual accumulation
of sulfate groups at the nonreducing terminus. Metabolically 35S-labeled TM was isolated from cultured rabbit heart endothelial
cells and characterized as a chondroitin sulfate proteoglycan which accounted for 1-2% of the total 35S-labeled cell-associated
macromolecules. The isolated chondroitin sulfate showed weaker antithrombin-dependent anticoagulant activity, on a molar basis,
than the intact TM proteoglycan. The anticoagulant action of TM thus depends on a unique form of functional collaboration
between the different constituents of a glycoconjugate.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)55414-4</identifier><identifier>PMID: 2168413</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>550201 - Biochemistry- Tracer Techniques ; ACETYLATION ; ACYLATION ; Analytical, structural and metabolic biochemistry ; ANIMAL TISSUES ; ANIMALS ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; BETA-MINUS DECAY RADIOISOTOPES ; Biological and medical sciences ; BODY ; CELL CULTURES ; Cells, Cultured ; CHEMICAL COMPOSITION ; CHEMICAL REACTIONS ; Chondroitin Lyases ; chondroitin sulfate ; CHROMATOGRAPHY ; Chromatography, Gel ; Chromatography, Ion Exchange ; DAYS LIVING RADIOISOTOPES ; Electrophoresis, Paper ; ENDOTHELIUM ; Endothelium - metabolism ; ENZYMES ; EVEN-ODD NUCLEI ; Fundamental and applied biological sciences. Psychology ; GLYCOPROTEINS ; Glycosaminoglycans - biosynthesis ; Glycosaminoglycans - isolation & purification ; Glycosaminoglycans - metabolism ; ION EXCHANGE CHROMATOGRAPHY ; ISOTOPE APPLICATIONS ; ISOTOPE DILUTION ; ISOTOPES ; LIGHT NUCLEI ; LYASES ; MAMMALS ; NUCLEI ; ORGANIC COMPOUNDS ; OXYGEN COMPOUNDS ; PROTEINS ; proteoglycans ; RABBITS ; Radioisotope Dilution Technique ; RADIOISOTOPES ; Receptors, Cell Surface - biosynthesis ; Receptors, Cell Surface - isolation & purification ; Receptors, Cell Surface - metabolism ; Receptors, Thrombin ; SEPARATION PROCESSES ; SULFATES ; Sulfates - metabolism ; SULFUR 35 ; SULFUR COMPOUNDS ; SULFUR ISOTOPES ; Sulfur Radioisotopes ; Thrombin - metabolism ; TISSUES ; TRACER TECHNIQUES ; Tritium ; VERTEBRATES</subject><ispartof>The Journal of biological chemistry, 1990-09, Vol.265 (26), p.15424-15431</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c468t-b74aa991e7283eb59396d5d59941d6abfe320f3159cddebef7bc38d7e49a1d533</citedby><cites>FETCH-LOGICAL-c468t-b74aa991e7283eb59396d5d59941d6abfe320f3159cddebef7bc38d7e49a1d533</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19436114$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2168413$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/6511778$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Bourin, M-C</creatorcontrib><creatorcontrib>Lundgren-Aakerlund, E</creatorcontrib><creatorcontrib>Lindahl, U</creatorcontrib><title>Isolation and characterization of the glycosaminoglycan component of rabbit thrombomodulin proteoglycan</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Previous studies on rabbit thrombomodulin (TM) revealed that certain anticoagulant activities expressed by TM depend on the
presence of an acidic domain tentatively identified as a sulfated galactosaminoglycan (Bourin, M.-C., Ohlin, A.-K., Lane,
D., Stenflo, J., and Lindahl, U. (1988) J. Biol. Chem. 263, 8044-8052). The glycan was released by alkaline beta-elimination,
isolated by ion-exchange chromatography, and radiolabeled by partial N-deacetylation (hydrazinolysis) followed by re-N-[3H]acetylation.
The labeled product behaved like standard chondroitin sulfate on ion-exchange chromatography, exhibited a Mr of 10-12 x 10(3)
on gel chromatography, and was susceptible to degradation by chondroitinase and testicular hyaluronidase. The major labeled
degradation products following digestion of the glycosaminoglycan with chondroitinase were identified, depending on the incubation
conditions, either as 4/6-mono-O-sulfated, 4,5-unsaturated disaccharides (delta HexA-GalNAc(S] and N-acetylgalactosamine 4,6-di-O-sulfate
(GalcNAc (diS], the latter component accounting for approximately 25% of the total label, or as a major fraction of labeled
trisaccharide, with the predominant structure GalNAc(diS)-GlcA-GalNAc(diS). The terminal GalNAc(diS) unit (not substituted
at C3) was shown to be more susceptible to N-deacetylation during hydrazinolysis than were the internal GalNAc units (substituted
at C3), and thus was more extensively labeled, resulting in over-representation of this unit. It is concluded that rabbit
TM is a chondroitin sulfate proteoglycan, which carries a single glycan side chain characterized by an unusual accumulation
of sulfate groups at the nonreducing terminus. Metabolically 35S-labeled TM was isolated from cultured rabbit heart endothelial
cells and characterized as a chondroitin sulfate proteoglycan which accounted for 1-2% of the total 35S-labeled cell-associated
macromolecules. The isolated chondroitin sulfate showed weaker antithrombin-dependent anticoagulant activity, on a molar basis,
than the intact TM proteoglycan. The anticoagulant action of TM thus depends on a unique form of functional collaboration
between the different constituents of a glycoconjugate.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>ACETYLATION</subject><subject>ACYLATION</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>ANIMAL TISSUES</subject><subject>ANIMALS</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BETA-MINUS DECAY RADIOISOTOPES</subject><subject>Biological and medical sciences</subject><subject>BODY</subject><subject>CELL CULTURES</subject><subject>Cells, Cultured</subject><subject>CHEMICAL COMPOSITION</subject><subject>CHEMICAL REACTIONS</subject><subject>Chondroitin Lyases</subject><subject>chondroitin sulfate</subject><subject>CHROMATOGRAPHY</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>Electrophoresis, Paper</subject><subject>ENDOTHELIUM</subject><subject>Endothelium - metabolism</subject><subject>ENZYMES</subject><subject>EVEN-ODD NUCLEI</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GLYCOPROTEINS</subject><subject>Glycosaminoglycans - biosynthesis</subject><subject>Glycosaminoglycans - isolation & purification</subject><subject>Glycosaminoglycans - metabolism</subject><subject>ION EXCHANGE CHROMATOGRAPHY</subject><subject>ISOTOPE APPLICATIONS</subject><subject>ISOTOPE DILUTION</subject><subject>ISOTOPES</subject><subject>LIGHT NUCLEI</subject><subject>LYASES</subject><subject>MAMMALS</subject><subject>NUCLEI</subject><subject>ORGANIC COMPOUNDS</subject><subject>OXYGEN COMPOUNDS</subject><subject>PROTEINS</subject><subject>proteoglycans</subject><subject>RABBITS</subject><subject>Radioisotope Dilution Technique</subject><subject>RADIOISOTOPES</subject><subject>Receptors, Cell Surface - biosynthesis</subject><subject>Receptors, Cell Surface - isolation & purification</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Thrombin</subject><subject>SEPARATION PROCESSES</subject><subject>SULFATES</subject><subject>Sulfates - metabolism</subject><subject>SULFUR 35</subject><subject>SULFUR COMPOUNDS</subject><subject>SULFUR ISOTOPES</subject><subject>Sulfur Radioisotopes</subject><subject>Thrombin - metabolism</subject><subject>TISSUES</subject><subject>TRACER TECHNIQUES</subject><subject>Tritium</subject><subject>VERTEBRATES</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV2L1TAQhoMo69nVn7BQRBe9qHaapE0uZfFjYcELFbwL-ZieRtrkmOQg66-33VPWSwNDwswzb154CbmE5i000L372jQt1LLl4jWIN5wzYDV7RHbQCFpTDj8ek90D8pSc5_yzWQ6TcEbOWugEA7oj-5scJ118DJUOrrKjTtoWTP7PqRmHqoxY7ac7G7OefYjrU4fKxvkQA4ayIkkb48tCpjibOEd3nHyoDikW3Phn5Mmgp4zPt_uCfP_44dv15_r2y6eb6_e3tWWdKLXpmdZSAvatoGi4pLJz3HEpGbhOmwFp2wwUuLTOocGhN5YK1yOTGhyn9IK8OOnGXLzK1he0o40hoC2q4wB9Lxbo6gQtDn8dMRc1-2xxmnTAeMyql1K0IJv_gsCFXAytID-BNsWcEw7qkPys052CRq1xqfu41JqFAqHu41Js2bvcPjiaGd3D1pbPMn-1zXW2ehqSDtbnf-KS0Q5g1Xl54ka_H3_7hMr4aEecVdvxpRanrGX0L8H1q1M</recordid><startdate>19900915</startdate><enddate>19900915</enddate><creator>Bourin, M-C</creator><creator>Lundgren-Aakerlund, E</creator><creator>Lindahl, U</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19900915</creationdate><title>Isolation and characterization of the glycosaminoglycan component of rabbit thrombomodulin proteoglycan</title><author>Bourin, M-C ; Lundgren-Aakerlund, E ; Lindahl, U</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c468t-b74aa991e7283eb59396d5d59941d6abfe320f3159cddebef7bc38d7e49a1d533</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>ACETYLATION</topic><topic>ACYLATION</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>ANIMAL TISSUES</topic><topic>ANIMALS</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BETA-MINUS DECAY RADIOISOTOPES</topic><topic>Biological and medical sciences</topic><topic>BODY</topic><topic>CELL CULTURES</topic><topic>Cells, Cultured</topic><topic>CHEMICAL COMPOSITION</topic><topic>CHEMICAL REACTIONS</topic><topic>Chondroitin Lyases</topic><topic>chondroitin sulfate</topic><topic>CHROMATOGRAPHY</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>Electrophoresis, Paper</topic><topic>ENDOTHELIUM</topic><topic>Endothelium - metabolism</topic><topic>ENZYMES</topic><topic>EVEN-ODD NUCLEI</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GLYCOPROTEINS</topic><topic>Glycosaminoglycans - biosynthesis</topic><topic>Glycosaminoglycans - isolation & purification</topic><topic>Glycosaminoglycans - metabolism</topic><topic>ION EXCHANGE CHROMATOGRAPHY</topic><topic>ISOTOPE APPLICATIONS</topic><topic>ISOTOPE DILUTION</topic><topic>ISOTOPES</topic><topic>LIGHT NUCLEI</topic><topic>LYASES</topic><topic>MAMMALS</topic><topic>NUCLEI</topic><topic>ORGANIC COMPOUNDS</topic><topic>OXYGEN COMPOUNDS</topic><topic>PROTEINS</topic><topic>proteoglycans</topic><topic>RABBITS</topic><topic>Radioisotope Dilution Technique</topic><topic>RADIOISOTOPES</topic><topic>Receptors, Cell Surface - biosynthesis</topic><topic>Receptors, Cell Surface - isolation & purification</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Thrombin</topic><topic>SEPARATION PROCESSES</topic><topic>SULFATES</topic><topic>Sulfates - metabolism</topic><topic>SULFUR 35</topic><topic>SULFUR COMPOUNDS</topic><topic>SULFUR ISOTOPES</topic><topic>Sulfur Radioisotopes</topic><topic>Thrombin - metabolism</topic><topic>TISSUES</topic><topic>TRACER TECHNIQUES</topic><topic>Tritium</topic><topic>VERTEBRATES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bourin, M-C</creatorcontrib><creatorcontrib>Lundgren-Aakerlund, E</creatorcontrib><creatorcontrib>Lindahl, U</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><collection>OSTI.GOV</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bourin, M-C</au><au>Lundgren-Aakerlund, E</au><au>Lindahl, U</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and characterization of the glycosaminoglycan component of rabbit thrombomodulin proteoglycan</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1990-09-15</date><risdate>1990</risdate><volume>265</volume><issue>26</issue><spage>15424</spage><epage>15431</epage><pages>15424-15431</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Previous studies on rabbit thrombomodulin (TM) revealed that certain anticoagulant activities expressed by TM depend on the
presence of an acidic domain tentatively identified as a sulfated galactosaminoglycan (Bourin, M.-C., Ohlin, A.-K., Lane,
D., Stenflo, J., and Lindahl, U. (1988) J. Biol. Chem. 263, 8044-8052). The glycan was released by alkaline beta-elimination,
isolated by ion-exchange chromatography, and radiolabeled by partial N-deacetylation (hydrazinolysis) followed by re-N-[3H]acetylation.
The labeled product behaved like standard chondroitin sulfate on ion-exchange chromatography, exhibited a Mr of 10-12 x 10(3)
on gel chromatography, and was susceptible to degradation by chondroitinase and testicular hyaluronidase. The major labeled
degradation products following digestion of the glycosaminoglycan with chondroitinase were identified, depending on the incubation
conditions, either as 4/6-mono-O-sulfated, 4,5-unsaturated disaccharides (delta HexA-GalNAc(S] and N-acetylgalactosamine 4,6-di-O-sulfate
(GalcNAc (diS], the latter component accounting for approximately 25% of the total label, or as a major fraction of labeled
trisaccharide, with the predominant structure GalNAc(diS)-GlcA-GalNAc(diS). The terminal GalNAc(diS) unit (not substituted
at C3) was shown to be more susceptible to N-deacetylation during hydrazinolysis than were the internal GalNAc units (substituted
at C3), and thus was more extensively labeled, resulting in over-representation of this unit. It is concluded that rabbit
TM is a chondroitin sulfate proteoglycan, which carries a single glycan side chain characterized by an unusual accumulation
of sulfate groups at the nonreducing terminus. Metabolically 35S-labeled TM was isolated from cultured rabbit heart endothelial
cells and characterized as a chondroitin sulfate proteoglycan which accounted for 1-2% of the total 35S-labeled cell-associated
macromolecules. The isolated chondroitin sulfate showed weaker antithrombin-dependent anticoagulant activity, on a molar basis,
than the intact TM proteoglycan. The anticoagulant action of TM thus depends on a unique form of functional collaboration
between the different constituents of a glycoconjugate.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2168413</pmid><doi>10.1016/S0021-9258(18)55414-4</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1990-09, Vol.265 (26), p.15424-15431 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_osti_scitechconnect_6511778 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | 550201 - Biochemistry- Tracer Techniques ACETYLATION ACYLATION Analytical, structural and metabolic biochemistry ANIMAL TISSUES ANIMALS BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES BETA-MINUS DECAY RADIOISOTOPES Biological and medical sciences BODY CELL CULTURES Cells, Cultured CHEMICAL COMPOSITION CHEMICAL REACTIONS Chondroitin Lyases chondroitin sulfate CHROMATOGRAPHY Chromatography, Gel Chromatography, Ion Exchange DAYS LIVING RADIOISOTOPES Electrophoresis, Paper ENDOTHELIUM Endothelium - metabolism ENZYMES EVEN-ODD NUCLEI Fundamental and applied biological sciences. Psychology GLYCOPROTEINS Glycosaminoglycans - biosynthesis Glycosaminoglycans - isolation & purification Glycosaminoglycans - metabolism ION EXCHANGE CHROMATOGRAPHY ISOTOPE APPLICATIONS ISOTOPE DILUTION ISOTOPES LIGHT NUCLEI LYASES MAMMALS NUCLEI ORGANIC COMPOUNDS OXYGEN COMPOUNDS PROTEINS proteoglycans RABBITS Radioisotope Dilution Technique RADIOISOTOPES Receptors, Cell Surface - biosynthesis Receptors, Cell Surface - isolation & purification Receptors, Cell Surface - metabolism Receptors, Thrombin SEPARATION PROCESSES SULFATES Sulfates - metabolism SULFUR 35 SULFUR COMPOUNDS SULFUR ISOTOPES Sulfur Radioisotopes Thrombin - metabolism TISSUES TRACER TECHNIQUES Tritium VERTEBRATES |
| title | Isolation and characterization of the glycosaminoglycan component of rabbit thrombomodulin proteoglycan |
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