Characterization of a Novel Sulfated Carbohydrate Unit Implicated in the Carbohydrate­Carbohydrate-mediated Cell Aggregation of the Marine Sponge Microciona prolifera

↓ Direkt till sidans innehåll
↓ Direkt till sidans sekundära innehåll (sidomenyn)

Sökning: WFRF:(Burger M.M.) > Characterization of...

5 av 5
Föregående post
Nästa post
Till träfflistan

LIBRIS Formathandbok (Information om MARC21)

Fältnamn	Indikatorer	Metadata
000		02887naa a2200325 4500
001		oai:DiVA.org:uu-52622
003		SwePub
008		081017s1995 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-526222 URI
040		a (SwePub)uu
041		a engb eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Spillmann, Dorotheu University of Turku4 aut0 (Swepub:uu)dsp11476
245	1 0	a Characterization of a Novel Sulfated Carbohydrate Unit Implicated in the CarbohydrateCarbohydrate-mediated Cell Aggregation of the Marine Sponge Microciona prolifera
264	1	c 1995
338		a print2 rdacarrier
520		a Species-specific cell reaggregation in the marine sponge Microciona prolifera is mediated by an adhesion proteoglycan. Two interactions are involved in the process: a Ca(2+)-dependent homophilic binding between proteoglycan molecules and a Ca(2+)-independent binding between the molecule and cells. Both interactions are mediated by the glycan moieties of the proteoglycan. The interaction of the proteoglycan with itself has been characterized as a carbohydrate-carbohydrate interaction of multiple low affinity sites. The monoclonal antibodies Block 1 and Block 2 raised against the purified aggregation proteoglycan and selected for inhibition of aggregation bind to these glycans. In a previous report the structure, [formula: see text] was assigned to the oligosaccharide reacting with Block 1 antibody (Spillmann, D., Hård, K., Thomas-Oates, J., Vliegenthart, J. F. G., Misevic, G., Burger, M. M., and Finne, J. (1993) J. Biol. Chem. 268, 13378-13387). By the technique of attaching the water-soluble acid-degraded fragments to a lipid carrier for immunochemical detection and by chemical, enzymatic and spectroscopic methods the structure, [formula: see text] was assigned to the oligosaccharide reacting with the aggregation-blocking monoclonal antibody Block 2. The structure, [formula: see text] was assigned to a major nonreactive oligosaccharide, which outlined the molecular requirements of antibody binding of the two aggregation-associated epitopes. These data demonstrate that two different functional sites with distinct structural characteristics and antibody reactivities are involved in the reaggregation of sponge cells, a model of carbohydrate-carbohydrate-mediated cell interactions.
653		a MEDICINE
653		a MEDICIN
700	1	a Thomas-Oates, J.E.4 aut
700	1	a van Kuik, A4 aut
700	1	a Vliegenhart, J.F.G.4 aut
700	1	a Misevic, G4 aut
700	1	a Burger, M.M.4 aut
700	1	a Finne, J4 aut
710	2	a University of Turku4 org
773	0	t Journal of Biological Chemistryg 270, s. 5089-5097q 270<5089-5097x 0021-9258x 1083-351X
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-52622

Hitta via bibliotek

Journal of Biological Chemistry (Sök värdpublikationen i LIBRIS)

Till lärosätets databas

5 av 5
Föregående post
Nästa post
Till träfflistan

Hitta mer i SwePub

Av författaren/redakt...: Spillmann, Dorot ...; Thomas-Oates, J. ...; van Kuik, A; Vliegenhart, J.F ...; Misevic, G; Burger, M.M.; visa fler...; Finne, J; visa färre...

Artiklar i publikationen: Journal of Biolo ...

Av lärosätet: Uppsala universitet

Sök utanför SwePub

Sök vidare i:: Google; Google Book Search; Google Scholar

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

LIBRIS.kb.se