File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1042/bj2220627
- Scopus: eid_2-s2.0-0021145407
- PMID: 6487266
- WOS: WOS:A1984TL25200008
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Effect of lead ions on chick-embryo liver mitochondrial δ-aminolaevulinate synthase
Title | Effect of lead ions on chick-embryo liver mitochondrial δ-aminolaevulinate synthase |
---|---|
Authors | |
Issue Date | 1984 |
Publisher | Portland Press Ltd. The Journal's web site is located at http://www.biochemj.org |
Citation | Biochemical Journal, 1984, v. 222 n. 3, p. 627-630 How to Cite? |
Abstract | Pb2+ activated native chick-embryo liver mitochondrial δ-aminolaevulinate synthase (EC 2.3.1.37). This result contradicted with the inhibitory effect observed by earlier workers who used degraded enzyme preparations. Enzyme activation was biphasic. An initial activation phase was observed with Pb2+ concentrations up to 200 μM, and a secondary phase with concentrations from 200 μM to at least 2 mM. Maximum primary activation was 2.5-fold at 200 μM-Pb2+, with a further 2-fold activation observed at 2 mM-Pb2+. Primary activation was not affected by a 10-fold molar excess of dithioerythritol, but the secondary activation was abolished by dithioerythritol. Secondary-phase activation was lost upon increasing time of incubation of the enzyme with Pb2+. The implications of these findings are discussed with reference to lead poisoning and the mechanism of δ-aminolaevulinate synthase. |
Persistent Identifier | http://hdl.handle.net/10722/147740 |
ISSN | 2023 Impact Factor: 4.4 2023 SCImago Journal Rankings: 1.612 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Pirola, BA | en_US |
dc.contributor.author | Borthwick, IA | en_US |
dc.contributor.author | Srivastava, G | en_US |
dc.date.accessioned | 2012-05-29T06:09:00Z | - |
dc.date.available | 2012-05-29T06:09:00Z | - |
dc.date.issued | 1984 | en_US |
dc.identifier.citation | Biochemical Journal, 1984, v. 222 n. 3, p. 627-630 | en_US |
dc.identifier.issn | 0264-6021 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/147740 | - |
dc.description.abstract | Pb2+ activated native chick-embryo liver mitochondrial δ-aminolaevulinate synthase (EC 2.3.1.37). This result contradicted with the inhibitory effect observed by earlier workers who used degraded enzyme preparations. Enzyme activation was biphasic. An initial activation phase was observed with Pb2+ concentrations up to 200 μM, and a secondary phase with concentrations from 200 μM to at least 2 mM. Maximum primary activation was 2.5-fold at 200 μM-Pb2+, with a further 2-fold activation observed at 2 mM-Pb2+. Primary activation was not affected by a 10-fold molar excess of dithioerythritol, but the secondary activation was abolished by dithioerythritol. Secondary-phase activation was lost upon increasing time of incubation of the enzyme with Pb2+. The implications of these findings are discussed with reference to lead poisoning and the mechanism of δ-aminolaevulinate synthase. | en_US |
dc.language | eng | en_US |
dc.publisher | Portland Press Ltd. The Journal's web site is located at http://www.biochemj.org | en_US |
dc.relation.ispartof | Biochemical Journal | en_US |
dc.subject.mesh | 5-Aminolevulinate Synthetase - Metabolism | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Chick Embryo | en_US |
dc.subject.mesh | Dithioerythritol - Pharmacology | en_US |
dc.subject.mesh | Enzyme Activation - Drug Effects | en_US |
dc.subject.mesh | Lead - Pharmacology | en_US |
dc.subject.mesh | Mitochondria, Liver - Enzymology | en_US |
dc.subject.mesh | Time Factors | en_US |
dc.title | Effect of lead ions on chick-embryo liver mitochondrial δ-aminolaevulinate synthase | en_US |
dc.type | Article | en_US |
dc.identifier.email | Srivastava, G:gopesh@pathology.hku.hk | en_US |
dc.identifier.authority | Srivastava, G=rp00365 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1042/bj2220627 | - |
dc.identifier.pmid | 6487266 | - |
dc.identifier.scopus | eid_2-s2.0-0021145407 | en_US |
dc.identifier.volume | 222 | en_US |
dc.identifier.issue | 3 | en_US |
dc.identifier.spage | 627 | en_US |
dc.identifier.epage | 630 | en_US |
dc.identifier.isi | WOS:A1984TL25200008 | - |
dc.publisher.place | United Kingdom | en_US |
dc.identifier.issnl | 0264-6021 | - |