Comparative studies on soluble and immobilized rabbit muscle pyruvate kinase

L. M. Simon, M. Kotormán, B. Szajáni, L. Boross

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Rabbit muscle pyruvate kinase was immobilized by covalent attachment to a polyacrylamide support (Akrilex C) containing carboxylic functional groups. As a result of immobilization, the pH optimum for catalytic activity shifted into a more alkaline direction. The apparent K m value with phosphoenolpyruvate increased, and that with ADP slightly decreased. With respect to the stability against urea and thermal inactivation, the immobilized pyruvate kinase seemed to be the more stable at lower urea concentrations and between 45 and 55°C. At 1.5 and 2.5M urea and at higher temperature, there were no marked differences between the soluble and the immobilized enzyme.

Original languageEnglish
Pages (from-to)195-205
Number of pages11
JournalApplied Biochemistry and Biotechnology
Volume11
Issue number3
DOIs
Publication statusPublished - Jun 1 1985

Keywords

  • Pyruvate kinase, soluble and immobilized
  • catalytic properties, and stability of immobilized pyruvate kinase
  • covalent coupling, of pyruvate kinase to Akrilex C
  • kinase, soluble and immobilized pyruvate
  • muscle pyruvate kinase, soluble and immobilized
  • rabbit muscle, soluble and immobilized rabbitmuscle from

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology

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