Matches in SemOpenAlex for { <https://semopenalex.org/work/W1517524532> ?p ?o ?g. }
Showing items 1 to 85 of
85
with 100 items per page.
- W1517524532 endingPage "9149" @default.
- W1517524532 startingPage "9146" @default.
- W1517524532 abstract "Although 2-O-sulfated L-iduronic acid (IdoA) residues have been known to occur in heparin, 2-O-sulfated D-glucuronic acid (GlcA) residues have been reported only recently (Bienkowski, M. J., and Conrad, H. E. (1985) J. Biol. Chem. 250, 356-365). Disaccharides prepared by cleavage of heparin and N-deacetylated chondroitin 6-sulfate with nitrous acid were used to demonstrate a new sulfatase that catalyzed the removal of the 2-O-sulfate substituents from GlcA but not IdoA residues. The deamination products were labeled by NaB3H4 reduction to give disaccharides from heparin and chondroitin sulfate which had reducing terminal 2,5-anhydro-D-mannitol ([3H]AManR) and 2,5-anhydro-D-talitol ([3H]ATalR) residues, respectively. IdoA(2-SO4)-[3H]AManR(6-SO4) from heparin and GlcA(2-SO4)-[3H]ATalR(6-SO4) from chondroitin sulfate were purified for use as substrates. GlcA(2-SO4)-[3H]AManR(6-SO4) was prepared by epimerization of IdoA(2-SO4)-[3H]AManR(6-SO4) with hydrazine at 100 degrees C. Lysosomal enzyme preparations from chick embryo chondrocytes and from two normal human fibroblast cell lines catalyzed the removal of the 2-O-SO4 substituent from the uronic acid residues of IdoA(2-SO4)-[3H]AManR(6-SO4), GlcA(2-SO4)-[3H] AManR(6-SO4), and GlcA(2-SO4)-[3H]ATalR(6-SO4). In contrast, a lysosomal enzyme preparation from a human fibroblast cell line deficient in idurono-2-sulfatase (Hunter's-syndrome), which had no activity on the IdoA(2-SO4)-[3H]AManR(6-SO4), converted GlcA(2-SO4)-[3H]AManR(6-SO4) to a mixture of GlcA-[3H] AManR(6-SO4) and [3H]AManR(6-SO4). This enzyme also converted GlcA(2-SO4)-[3H]ATalR(6-SO4) to a mixture of GlcA-[3H]ATalR(6-SO4) and [3H]ATalR(6-SO4). Digestion of both GlcA(2-SO4)-[3H]AManR(6-SO4) and GlcA(2-SO4)-[3H]ATalR(6-SO4) was inhibited by 35SO2-4 and was arrested at the monosulfated disaccharide stage by 1,4-saccharolactone. The glucurono-2-sulfatase exhibited a pH optimum of 4. The results indicate that there exists a separate sulfatase for the removal of sulfate substituents from C-2 of GlcA residues in glycosaminoglycans." @default.
- W1517524532 created "2016-06-24" @default.
- W1517524532 creator A5026367825 @default.
- W1517524532 creator A5040344520 @default.
- W1517524532 creator A5076590505 @default.
- W1517524532 date "1985-08-01" @default.
- W1517524532 modified "2023-09-27" @default.
- W1517524532 title "A sulfatase specific for glucuronic acid 2-sulfate residues in glycosaminoglycans." @default.
- W1517524532 cites W1503648662 @default.
- W1517524532 cites W1507064897 @default.
- W1517524532 cites W1594150232 @default.
- W1517524532 cites W1629226911 @default.
- W1517524532 cites W1979269268 @default.
- W1517524532 cites W1982566089 @default.
- W1517524532 cites W1996249803 @default.
- W1517524532 cites W2005327727 @default.
- W1517524532 cites W2038363212 @default.
- W1517524532 cites W2038934672 @default.
- W1517524532 cites W2078657338 @default.
- W1517524532 cites W2083718300 @default.
- W1517524532 cites W2089515940 @default.
- W1517524532 cites W2091094259 @default.
- W1517524532 cites W2111065678 @default.
- W1517524532 cites W2173078011 @default.
- W1517524532 cites W2420290734 @default.
- W1517524532 doi "https://doi.org/10.1016/s0021-9258(17)39342-0" @default.
- W1517524532 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/4019466" @default.
- W1517524532 hasPublicationYear "1985" @default.
- W1517524532 type Work @default.
- W1517524532 sameAs 1517524532 @default.
- W1517524532 citedByCount "26" @default.
- W1517524532 countsByYear W15175245322012 @default.
- W1517524532 countsByYear W15175245322015 @default.
- W1517524532 countsByYear W15175245322016 @default.
- W1517524532 countsByYear W15175245322017 @default.
- W1517524532 countsByYear W15175245322020 @default.
- W1517524532 countsByYear W15175245322022 @default.
- W1517524532 crossrefType "journal-article" @default.
- W1517524532 hasAuthorship W1517524532A5026367825 @default.
- W1517524532 hasAuthorship W1517524532A5040344520 @default.
- W1517524532 hasAuthorship W1517524532A5076590505 @default.
- W1517524532 hasBestOaLocation W15175245321 @default.
- W1517524532 hasConcept C100817775 @default.
- W1517524532 hasConcept C153074725 @default.
- W1517524532 hasConcept C178790620 @default.
- W1517524532 hasConcept C181199279 @default.
- W1517524532 hasConcept C185592680 @default.
- W1517524532 hasConcept C2776648616 @default.
- W1517524532 hasConcept C2778041096 @default.
- W1517524532 hasConcept C2778343803 @default.
- W1517524532 hasConcept C2780871851 @default.
- W1517524532 hasConcept C2910763122 @default.
- W1517524532 hasConcept C55493867 @default.
- W1517524532 hasConceptScore W1517524532C100817775 @default.
- W1517524532 hasConceptScore W1517524532C153074725 @default.
- W1517524532 hasConceptScore W1517524532C178790620 @default.
- W1517524532 hasConceptScore W1517524532C181199279 @default.
- W1517524532 hasConceptScore W1517524532C185592680 @default.
- W1517524532 hasConceptScore W1517524532C2776648616 @default.
- W1517524532 hasConceptScore W1517524532C2778041096 @default.
- W1517524532 hasConceptScore W1517524532C2778343803 @default.
- W1517524532 hasConceptScore W1517524532C2780871851 @default.
- W1517524532 hasConceptScore W1517524532C2910763122 @default.
- W1517524532 hasConceptScore W1517524532C55493867 @default.
- W1517524532 hasIssue "16" @default.
- W1517524532 hasLocation W15175245321 @default.
- W1517524532 hasOpenAccess W1517524532 @default.
- W1517524532 hasPrimaryLocation W15175245321 @default.
- W1517524532 hasRelatedWork W1963551574 @default.
- W1517524532 hasRelatedWork W1963935916 @default.
- W1517524532 hasRelatedWork W1975691939 @default.
- W1517524532 hasRelatedWork W1995136808 @default.
- W1517524532 hasRelatedWork W2027074537 @default.
- W1517524532 hasRelatedWork W2080004275 @default.
- W1517524532 hasRelatedWork W2089186041 @default.
- W1517524532 hasRelatedWork W2095409487 @default.
- W1517524532 hasRelatedWork W2096702246 @default.
- W1517524532 hasRelatedWork W4211263999 @default.
- W1517524532 hasVolume "260" @default.
- W1517524532 isParatext "false" @default.
- W1517524532 isRetracted "false" @default.
- W1517524532 magId "1517524532" @default.
- W1517524532 workType "article" @default.