Immobilized citrate synthase

Amal Mukherjee, Paul A. Srere

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Kinetic properties of pig heart citrate synthase immobilized on Sepharose were determined. Compared to the free enzyme the Km values for both acetyl-CoA and oxalacetate were increased. The kinetic pattern of the Lineweaver-Burk plots of both substrates for the immobilized enzyme was that of lines intersecting on the x axis. This is the same as that obtained for the free enzyme and indicates that there is no change in the kinetic mechanism of the reaction. The pH response and the Arrhenius plot of both the immobilized and free enzyme were the same. The enzymes show a break in their Arrhenius plots. The immobilized enzyme exhibits greater heat stability than does the free enzyme.

Original languageEnglish
Pages (from-to)85-94
Number of pages10
JournalJournal of Solid-Phase Biochemistry
Volume3
Issue number1
DOIs
Publication statusPublished - Mar 1 1978

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ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Applied Microbiology and Biotechnology

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