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- Publisher Website: 10.1006/bbrc.1993.1265
- Scopus: eid_2-s2.0-0027240645
- PMID: 8461019
- WOS: WOS:A1993KT12800046
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Article: Production and hydrolysis of cyclic ADP-ribose at the outer surface of human erythrocytes
Title | Production and hydrolysis of cyclic ADP-ribose at the outer surface of human erythrocytes |
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Authors | |
Issue Date | 1993 |
Publisher | Academic 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. 191 n. 2, p. 639-645 How to Cite? |
Abstract | Hemoglobin-free membranes from human erythrocytes are able to convert β- NAD+ to cyclic ADP-ribose, a calcium mobilizer as potent as inositol 1,4,5- trisphosphate. Identification of cyclic ADP-ribose was based on HPLC analyses and its Ca2+-mobilizing activity on sea urchin egg microsomes. Erythrocyte membranes also hydrolyze cyclic ADP-ribose to ADP-ribose. By comparing the cyclic ADP-ribose-synthesizing and hydrolyzing activities on unsealed and right-side-out resealed ghosts, it can be concluded that both are localized at the extracellular side of the membrane. This is confirmed by the demonstration of both enzyme activities on the surface of intact human red cells. Identification of the two enzymes involved in cyclic ADP-ribose metabolism might suggest some physiological role of this nucleotide in red cells. |
Persistent Identifier | http://hdl.handle.net/10722/171575 |
ISSN | 2021 Impact Factor: 3.322 2020 SCImago Journal Rankings: 0.998 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Hon Cheung Lee | en_US |
dc.contributor.author | Zocchi, E | en_US |
dc.contributor.author | Guida, L | en_US |
dc.contributor.author | Franco, L | en_US |
dc.contributor.author | Benatti, U | en_US |
dc.contributor.author | De Flora, A | en_US |
dc.date.accessioned | 2012-10-30T06:15:45Z | - |
dc.date.available | 2012-10-30T06:15:45Z | - |
dc.date.issued | 1993 | en_US |
dc.identifier.citation | Biochemical And Biophysical Research Communications, 1993, v. 191 n. 2, p. 639-645 | en_US |
dc.identifier.issn | 0006-291X | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171575 | - |
dc.description.abstract | Hemoglobin-free membranes from human erythrocytes are able to convert β- NAD+ to cyclic ADP-ribose, a calcium mobilizer as potent as inositol 1,4,5- trisphosphate. Identification of cyclic ADP-ribose was based on HPLC analyses and its Ca2+-mobilizing activity on sea urchin egg microsomes. Erythrocyte membranes also hydrolyze cyclic ADP-ribose to ADP-ribose. By comparing the cyclic ADP-ribose-synthesizing and hydrolyzing activities on unsealed and right-side-out resealed ghosts, it can be concluded that both are localized at the extracellular side of the membrane. This is confirmed by the demonstration of both enzyme activities on the surface of intact human red cells. Identification of the two enzymes involved in cyclic ADP-ribose metabolism might suggest some physiological role of this nucleotide in red cells. | en_US |
dc.language | eng | en_US |
dc.publisher | Academic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description | en_US |
dc.relation.ispartof | Biochemical and Biophysical Research Communications | en_US |
dc.subject.mesh | Adp-Ribosyl Cyclase | en_US |
dc.subject.mesh | Adenosine Diphosphate Ribose - Analogs & Derivatives - Biosynthesis - Metabolism | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Antigens, Cd | en_US |
dc.subject.mesh | Antigens, Cd38 | en_US |
dc.subject.mesh | Antigens, Differentiation - Metabolism | en_US |
dc.subject.mesh | Calcium - Metabolism | en_US |
dc.subject.mesh | Cells, Cultured | en_US |
dc.subject.mesh | Cyclic Adp-Ribose | en_US |
dc.subject.mesh | Erythrocyte Membrane - Metabolism | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Hydrolysis | en_US |
dc.subject.mesh | Membrane Glycoproteins | en_US |
dc.subject.mesh | Microsomes - Metabolism | en_US |
dc.subject.mesh | N-Glycosyl Hydrolases - Metabolism | en_US |
dc.subject.mesh | Nad - Metabolism | en_US |
dc.subject.mesh | Ovum | en_US |
dc.subject.mesh | Sea Urchins | en_US |
dc.title | Production and hydrolysis of cyclic ADP-ribose at the outer surface of human erythrocytes | en_US |
dc.type | Article | en_US |
dc.identifier.email | Hon Cheung Lee:leehc@hku.hk | en_US |
dc.identifier.authority | Hon Cheung Lee=rp00545 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1006/bbrc.1993.1265 | en_US |
dc.identifier.pmid | 8461019 | - |
dc.identifier.scopus | eid_2-s2.0-0027240645 | en_US |
dc.identifier.volume | 191 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.spage | 639 | en_US |
dc.identifier.epage | 645 | en_US |
dc.identifier.isi | WOS:A1993KT12800046 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Hon Cheung Lee=26642959100 | en_US |
dc.identifier.scopusauthorid | Zocchi, E=7003441674 | en_US |
dc.identifier.scopusauthorid | Guida, L=7006059917 | en_US |
dc.identifier.scopusauthorid | Franco, L=35412467500 | en_US |
dc.identifier.scopusauthorid | Benatti, U=7005696019 | en_US |
dc.identifier.scopusauthorid | De Flora, A=7006450815 | en_US |
dc.identifier.issnl | 0006-291X | - |