Recovery of active, highly purified phosphoenolpyruvate carboxylase from specific immunoadsorbent column
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چکیده
منابع مشابه
The Effect of Adenine Nucleotides on Purified Phosphoenolpyruvate Carboxylase from the CAM Plant Crassula argentea.
The effects of adenine nucleotides on phosphoenolypyruvate carboxylase were investigated using purified enzyme from the CAM plant, Crassula argentea. At 1 millimolar total concentration and with limiting phosphoenolpyruvate, AMP had a stimulatory effect, lowering the K(m) for phosphoenolpyruvate, ADP caused less stimulation, and ATP decreased the activity by increasing the K(m) for phosphoenolp...
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Phosphoenolpyruvate carboxylase partially purified from leaves of Crassula and rendered insensitive to malate by storage without adjuvants can be altered to the form sensitive to malate inhibition by brief, 5-minute preincubation with 5 millimolar malate. The induction of malate sensitivity is reversible by lowering the malate2concentration. Of the reaction components only HC03increases the sen...
متن کاملPHOSPHOENOLPYRUVATE CARBOXYLASE: A Ubiquitous, Highly Regulated Enzyme in Plants.
Since plant phosphoenolpyruvate carboxylase (PEPC) was last reviewed in the Annual Review of Plant Physiology over a decade ago (O'Leary 1982), significant advances have been made in our knowledge of this oligomeric, cytosolic enzyme. This review highlights this exciting progress in plant PEPC research by focusing on the three major areas of recent investigation: the enzymology of the protein; ...
متن کاملCloning and sequence analysis of cDNA encoding active phosphoenolpyruvate carboxylase of the C4-pathway from maize.
A recombinant clone, pM52, containing cDNA for maize phosphoenolpyruvate carboxylase (PEPCase, EC 4.1.1.31) was isolated from a maize leaf cDNA library constructed using an expression vector in Escherichia coli. The screening of the clone was conveniently performed through its ability to complement the phenotype (glutamate requirement) of PEPCase-negative mutant of E. coli. The enzyme encoded b...
متن کاملPurification and characterization of phosphoenolpyruvate carboxylase from Plasmodium berghei.
Phosphoenolpyruvate (PEP) carboxylase was purified over 400-fold from Plasmodium berghei. The purified enzyme was stable in 0.4 m potassium phosphate buffer (pH 7.4) containing 0.5 m glucose, 1 mm ethylenediaminetetraacetic acid (EDTA), and 1 mm MgCl(2). It had a molecular weight of 280,000 determined by sucrose density gradient centrifugation in this buffer, but it aggregated and was unstable ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1980
ISSN: 0014-5793
DOI: 10.1016/0014-5793(80)81211-7