Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Proteolytic modification of pig and rat liver pyruvate kinase including the phosphorylatable site
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk och fysiologisk kemi. (Engström Lorentz)
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk och fysiologisk kemi. (Engström Lorentz)
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk och fysiologisk kemi. (Engström Lorentz)
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk och fysiologisk kemi. (Engström Lorentz)
1978 (engelsk)Inngår i: Biochimica et Biophysica Acta, ISSN 0006-3002, E-ISSN 1878-2434, Vol. 532, nr 2, s. 259-267Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
1978. Vol. 532, nr 2, s. 259-267
HSV kategori
Identifikatorer
URN: urn:nbn:se:uu:diva-169192PubMedID: 623783OAI: oai:DiVA.org:uu-169192DiVA, id: diva2:505408
Tilgjengelig fra: 2012-02-23 Laget: 2012-02-23 Sist oppdatert: 2018-01-12bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

PubMed

Søk i DiVA

Av forfatter/redaktør
Ekman, Pia
Av organisasjonen
I samme tidsskrift
Biochimica et Biophysica Acta

Søk utenfor DiVA

GoogleGoogle Scholar

pubmed
urn-nbn

Altmetric

pubmed
urn-nbn
Totalt: 446 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf