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Article: A single protein immunologically identified as CD38 displays NAD+ glycohydrolase, ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities at the outer surface of human erythrocytes

TitleA single protein immunologically identified as CD38 displays NAD+ glycohydrolase, ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities at the outer surface of human erythrocytes
Authors
Zocchi, EFranco, LGuida, LBenatti, UBargellesi, AMalavasi, FLee, HCDe Flora, A
Issue Date1993
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
Citation
Biochemical And Biophysical Research Communications, 1993, v. 196 n. 3, p. 1459-1465 How to Cite?
DOI: http://dx.doi.org/10.1006/bbrc.1993.2416
AbstractThe three ectoenzyme activities, NAD+ glycohydrolase, ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase were purified to homogeneity from solubilized human erythrocyte membranes. The purification procedure involved three sequential chromatography steps on hydroxylapatite, immobilized Cu++ and immobilized anti-CD38 monoclonal antibody resins. The final step yielded a single 46 kDa protein displaying all three enzymatic activities. Since the protein bound specifically to the anti-CD38 resin, it was immunologically identified as CD38, a 46 kDa surface antigen involved in activation and proliferation of lymphocyte populations.
Persistent Identifierhttp://hdl.handle.net/10722/171592
ISSN
0006-291X
2021 Impact Factor: 3.322
2020 SCImago Journal Rankings: 0.998
ISI Accession Number ID
WOS:A1993MG31000064

 

DC FieldValueLanguage
dc.contributor.authorZocchi, Een_US
dc.contributor.authorFranco, Len_US
dc.contributor.authorGuida, Len_US
dc.contributor.authorBenatti, Uen_US
dc.contributor.authorBargellesi, Aen_US
dc.contributor.authorMalavasi, Fen_US
dc.contributor.authorLee, HCen_US
dc.contributor.authorDe Flora, Aen_US
dc.date.accessioned2012-10-30T06:15:52Z-
dc.date.available2012-10-30T06:15:52Z-
dc.date.issued1993en_US
dc.identifier.citationBiochemical And Biophysical Research Communications, 1993, v. 196 n. 3, p. 1459-1465en_US
dc.identifier.issn0006-291Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/171592-
dc.description.abstractThe three ectoenzyme activities, NAD+ glycohydrolase, ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase were purified to homogeneity from solubilized human erythrocyte membranes. The purification procedure involved three sequential chromatography steps on hydroxylapatite, immobilized Cu++ and immobilized anti-CD38 monoclonal antibody resins. The final step yielded a single 46 kDa protein displaying all three enzymatic activities. Since the protein bound specifically to the anti-CD38 resin, it was immunologically identified as CD38, a 46 kDa surface antigen involved in activation and proliferation of lymphocyte populations.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/descriptionen_US
dc.relation.ispartofBiochemical and Biophysical Research Communicationsen_US
dc.subject.meshAdp-Ribosyl Cyclaseen_US
dc.subject.meshAntigens, Cd - Blood - Isolation & Purificationen_US
dc.subject.meshAntigens, Cd38en_US
dc.subject.meshAntigens, Differentiation - Blood - Isolation & Purificationen_US
dc.subject.meshChlorides - Pharmacologyen_US
dc.subject.meshChromatographyen_US
dc.subject.meshCopper - Pharmacologyen_US
dc.subject.meshDurapatiteen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshErythrocyte Membrane - Enzymologyen_US
dc.subject.meshHumansen_US
dc.subject.meshKineticsen_US
dc.subject.meshMembrane Glycoproteinsen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshN-Glycosyl Hydrolases - Blood - Isolation & Purificationen_US
dc.subject.meshNad+ Nucleosidase - Blood - Isolation & Purificationen_US
dc.subject.meshZinc Compounds - Pharmacologyen_US
dc.titleA single protein immunologically identified as CD38 displays NAD+ glycohydrolase, ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities at the outer surface of human erythrocytesen_US
dc.typeArticleen_US
dc.identifier.emailLee, HC:leehc@hku.hken_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1006/bbrc.1993.2416en_US
dc.identifier.pmid8250903-
dc.identifier.scopuseid_2-s2.0-0027497231en_US
dc.identifier.volume196en_US
dc.identifier.issue3en_US
dc.identifier.spage1459en_US
dc.identifier.epage1465en_US
dc.identifier.isiWOS:A1993MG31000064-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridZocchi, E=7003441674en_US
dc.identifier.scopusauthoridFranco, L=35412467500en_US
dc.identifier.scopusauthoridGuida, L=7006059917en_US
dc.identifier.scopusauthoridBenatti, U=7005696019en_US
dc.identifier.scopusauthoridBargellesi, A=7003422297en_US
dc.identifier.scopusauthoridMalavasi, F=7004453948en_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US
dc.identifier.scopusauthoridDe Flora, A=7006450815en_US
dc.identifier.issnl0006-291X-

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