Rapid purification of pig heart fumarase by general ligand chromatography

Laura A. Halper, P. Srere

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

A rapid method for the purification of fumarase from pig heart muscle has been developed using general ligand chromatography with adenosine triphosphate as ligand. Fumarase exhibited distinctive elution patterns from several types of nucleotide-agarose matrices, which may prove of value in distinguishing putative isozymic forms. Fumarase purified from both soluble and particulate fractions of cardiac tissue appeared to be identical in terms of subunit molecular weight, electrophoretic mobility on cellulose acetate, substrate kinetics, and inactivation by several inhibitors. When fresh cardiac tissue was suspended in sucrose medium, both fumarase and citrate synthase were released from the mitochondria to about the same extent (10%). However, fumarase release was increased approximately three-fold, while the release of titrate synthase increased only slightly, when tissue which had been frozen and thawed was suspended in sucrose medium.

Original languageEnglish
Pages (from-to)1-13
Number of pages13
JournalJournal of Solid-Phase Biochemistry
Volume4
Issue number1
DOIs
Publication statusPublished - Mar 1979

Fingerprint

Fumarate Hydratase
Chromatography
Purification
Swine
Ligands
Tissue
Sucrose
Citrate (si)-Synthase
Electrophoretic mobility
Mitochondria
Sepharose
Muscle
Myocardium
Nucleotides
Adenosine Triphosphate
Molecular Weight
Molecular weight
Kinetics
Substrates

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Biotechnology
  • Biochemistry

Cite this

Rapid purification of pig heart fumarase by general ligand chromatography. / Halper, Laura A.; Srere, P.

In: Journal of Solid-Phase Biochemistry, Vol. 4, No. 1, 03.1979, p. 1-13.

Research output: Contribution to journalArticle

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