Journal article
Rat liver 4-hydroxy-2-ketoglutarate aldolase: Purification and kinetic characterization
Archives of biochemistry and biophysics, Vol.236(1), pp.82-97
1985
DOI: 10.1016/0003-9861(85)90608-3
PMID: 3966804
Abstract
The enzyme 4-hydroxy-2-ketoglutarate aldolase (4HKG aldolase), which catalyzes the reversible cleavage of 4-hydroxy-2-ketoglutarate to form pyruvate and glyoxylate, was isolated from rat liver. The purification scheme as well as a study of several of the physical and kinetic properties of the enzyme are presented. The effects of anions, various buffers, and possible physiologically relevant effectors on the kinetic parameters of the aldolase were also investigated. It was found that pyruvate analogs inhibited the aldolase. Oxaloacetate was a competitive inhibitor of the aldolase, and in addition caused synergistic inhibition with respect to pyruvate analogs at low substrate concentration. These results are discussed in terms of possible regulation of the aldolase.
Details
- Title: Subtitle
- Rat liver 4-hydroxy-2-ketoglutarate aldolase: Purification and kinetic characterization
- Creators
- Melissa Anderson - University of Nebraska–LincolnJohn M. Scholtz - University of Nebraska–LincolnSheldon M. Schuster - University of Nebraska–Lincoln
- Resource Type
- Journal article
- Publication Details
- Archives of biochemistry and biophysics, Vol.236(1), pp.82-97
- Publisher
- Elsevier Inc
- DOI
- 10.1016/0003-9861(85)90608-3
- PMID
- 3966804
- ISSN
- 0003-9861
- eISSN
- 1096-0384
- Language
- English
- Date published
- 1985
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984293085902771
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