Immobilization of pig muscle 3-phosphoglycerate kinase

L. M. Simon, J. Szelei, B. Szajáni, L. Boross

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

3-Phosphoglycerate kinase (ATP:3-phospho-d-glycerate 1-phosphotransferase, EC 2.7.2.3) has been covalently immobilized on a polyacrylamide-type support containing carboxylic groups activated by water-soluble carbodiimide. The activity was 88 units g-1 xerogel. The activity versus pH profile showed a sharper maximum at pH 6.5 in the case of the immobilized enzyme. The immobilized enzyme had a broad apparent optimum temperature range between 40 and 50°C. The apparent Km values of the immobilized 3-phosphoglycerate kinase were lower for both 3-phosphoglycerate and ATP than those of the soluble enzyme. In the case of the immobilized enzyme stabilities were enhanced.

Original languageEnglish
Pages (from-to)357-360
Number of pages4
JournalEnzyme and Microbial Technology
Volume7
Issue number7
DOIs
Publication statusPublished - Jul 1985

Keywords

  • Enzyme
  • catalytic properties
  • covalent attachment
  • immobilized 3-phosphoglycerate kinase
  • stability tests

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

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