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Ekman, Pia
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Bergström, G., Ekman, P., Humble, E. & Engström, L. (1978). Proteolytic modification of pig and rat liver pyruvate kinase including the phosphorylatable site. Biochimica et Biophysica Acta, 532(2), 259-267
Open this publication in new window or tab >>Proteolytic modification of pig and rat liver pyruvate kinase including the phosphorylatable site
1978 (English)In: Biochimica et Biophysica Acta, ISSN 0006-3002, E-ISSN 1878-2434, Vol. 532, no 2, p. 259-267Article in journal (Refereed) Published
Abstract [en]

The phosphorylated or phosphate-accepting site of pyruvate kinase from pig and rat liver was removed without inactivation by incubation with subtilisin. At different time intervals the subtilisin was inactivated with phenylmethylsulfonyl fluoride and the amount of remaining phosphorylatable or phosphorylated sites of pyruvate kinase estimated by incubation with an excess of [32P]-ATP and protein kinase. It was found that to get the same rate of modification the subtilisin concentration required to modify unphosphorylated pyruvate kinase was approximately ten times higher than that used for removal of the phosphorylated site of phosphorylated site of phosphorylated enzyme. It was shown that the proteolytically-modified pyruvate kinase had an increased apparent Km for phosphoenolpyruvate without a change in V, when compared to unmodified unphosphorylated and phosphorylated pyruvate kinase. The removal of the phosphorylated site was not associated with loss of the allosteric sites for ATP and Fru-1,6-P2. The possibility that phosphorylation of the pyruvate kinase increases its degradation rate in vivo is briefly discussed.

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Other Basic Medicine
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urn:nbn:se:uu:diva-169192 (URN)623783 (PubMedID)
Available from: 2012-02-23 Created: 2012-02-23 Last updated: 2018-01-12Bibliographically approved
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