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Article: Apparent inhibition of pyruvate kinase by phosphocreatine and phosphoarginine

TitleApparent inhibition of pyruvate kinase by phosphocreatine and phosphoarginine
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date1979
Citation
Comparative Biochemistry And Physiology, 1979, v. 63 n. 1 B, p. 29-34 How to Cite?
AbstractAddition of a non-dialysable, heat-labile and acid-precipitable factor which was not absorbed on DEAE-cellulose column, could restore the sensitivity of the chromatographed muscle pyruvate kinase from Marphysa sanguinea towards phosphocreatine inhibition. This factor, being non-specific as it acts on pyruvate kinase isozymes from different sources, demonstrated high creatine kinase activity. High concentrations of ADP, creatine or replacement of ADP with IDP/UDP or high pH abolished the inhibition indicating that the inhibition was mediated through creatine kinase by depleting ADP. Apparent inhibition of phosphocreatine was related to the relative activities of 3 intracellular enzymes-pyruvate kinase, creatine kinase and adenosine triphosphatase.
Persistent Identifierhttp://hdl.handle.net/10722/92451
ISSN
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWu, SWNen_HK
dc.contributor.authorWong, SCen_HK
dc.contributor.authorYeung, Den_HK
dc.date.accessioned2010-09-17T10:46:35Z-
dc.date.available2010-09-17T10:46:35Z-
dc.date.issued1979en_HK
dc.identifier.citationComparative Biochemistry And Physiology, 1979, v. 63 n. 1 B, p. 29-34en_HK
dc.identifier.issn0010-406Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/92451-
dc.description.abstractAddition of a non-dialysable, heat-labile and acid-precipitable factor which was not absorbed on DEAE-cellulose column, could restore the sensitivity of the chromatographed muscle pyruvate kinase from Marphysa sanguinea towards phosphocreatine inhibition. This factor, being non-specific as it acts on pyruvate kinase isozymes from different sources, demonstrated high creatine kinase activity. High concentrations of ADP, creatine or replacement of ADP with IDP/UDP or high pH abolished the inhibition indicating that the inhibition was mediated through creatine kinase by depleting ADP. Apparent inhibition of phosphocreatine was related to the relative activities of 3 intracellular enzymes-pyruvate kinase, creatine kinase and adenosine triphosphatase.en_HK
dc.languageengen_HK
dc.relation.ispartofComparative Biochemistry and Physiologyen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titleApparent inhibition of pyruvate kinase by phosphocreatine and phosphoarginineen_HK
dc.typeArticleen_HK
dc.identifier.emailWu, SWN: winninwu@hkucc.hku.hken_HK
dc.identifier.emailWong, SC: hhecwsc@hku.hken_HK
dc.identifier.authorityWu, SWN=rp01396en_HK
dc.identifier.authorityWong, SC=rp00191en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid318398-
dc.identifier.scopuseid_2-s2.0-0018428488en_HK
dc.identifier.volume63en_HK
dc.identifier.issue1 Ben_HK
dc.identifier.spage29en_HK
dc.identifier.epage34en_HK
dc.identifier.isiWOS:A1979GT39000006-
dc.identifier.scopusauthoridWu, SWN=7407184882en_HK
dc.identifier.scopusauthoridWong, SC=24323361400en_HK
dc.identifier.scopusauthoridYeung, D=7103391367en_HK

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