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Article: Biosynthesis of pyruvate kinase isozymes in rat liver.

TitleBiosynthesis of pyruvate kinase isozymes in rat liver.
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date1981
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJB
Citation
European Journal Of Biochemistry, 1981, v. 121 n. 1, p. 59-63 How to Cite?
Abstract1. The L and M1 isozymes of pyruvate kinase were purified to homogeneity from rat liver and muscle respectively and their specific antibodies were employed to quantify the isozyme concentration in rat liver during development. 2. Total enzyme activity decreases towards birth and reaches a minimum on the 3rd postnatal day, but the activity increases dramatically after weaning. 3. Immunoprecipitation revealed that the M2 type predominates in the prenatal period but decreases sharply just before birth. 4. The L isozyme contribution is augmented upon weaning and is sustained until the rat is adult and a L/M ratio of 9:1 is maintained. 5. By means of incorporation studies with [3H]leucine followed by immunoprecipitation, the increase in L-type activity when approaching term and after weaning is explained by a twofold increase in its rate of synthesis coupled with a concomitant reduction of the M2-type synthesis.
Persistent Identifierhttp://hdl.handle.net/10722/92454
ISSN
2006 Impact Factor: 3.579
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWu, SWen_HK
dc.contributor.authorWong, SSen_HK
dc.contributor.authorYeung, DCen_HK
dc.date.accessioned2010-09-17T10:46:40Z-
dc.date.available2010-09-17T10:46:40Z-
dc.date.issued1981en_HK
dc.identifier.citationEuropean Journal Of Biochemistry, 1981, v. 121 n. 1, p. 59-63en_HK
dc.identifier.issn0014-2956en_HK
dc.identifier.urihttp://hdl.handle.net/10722/92454-
dc.description.abstract1. The L and M1 isozymes of pyruvate kinase were purified to homogeneity from rat liver and muscle respectively and their specific antibodies were employed to quantify the isozyme concentration in rat liver during development. 2. Total enzyme activity decreases towards birth and reaches a minimum on the 3rd postnatal day, but the activity increases dramatically after weaning. 3. Immunoprecipitation revealed that the M2 type predominates in the prenatal period but decreases sharply just before birth. 4. The L isozyme contribution is augmented upon weaning and is sustained until the rat is adult and a L/M ratio of 9:1 is maintained. 5. By means of incorporation studies with [3H]leucine followed by immunoprecipitation, the increase in L-type activity when approaching term and after weaning is explained by a twofold increase in its rate of synthesis coupled with a concomitant reduction of the M2-type synthesis.en_HK
dc.languageengen_HK
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJBen_HK
dc.relation.ispartofEuropean Journal of Biochemistryen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titleBiosynthesis of pyruvate kinase isozymes in rat liver.en_HK
dc.typeArticleen_HK
dc.identifier.emailWu, SW: winninwu@hkucc.hku.hken_HK
dc.identifier.authorityWu, SW=rp01396en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid7327170-
dc.identifier.scopuseid_2-s2.0-0019757956en_HK
dc.identifier.volume121en_HK
dc.identifier.issue1en_HK
dc.identifier.spage59en_HK
dc.identifier.epage63en_HK
dc.identifier.isiWOS:A1981MU89200009-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridWu, SW=7407184882en_HK
dc.identifier.scopusauthoridWong, SS=36912444300en_HK
dc.identifier.scopusauthoridYeung, DC=7103391367en_HK

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