Artifacts in the assay of maize leaf phosphoenolpyruvate carboxylase activity due to its instability

1988 ◽  
Vol 18 (3) ◽  
pp. 317-325 ◽  
Author(s):  
K. Angelopoulos ◽  
K. Stamatakis ◽  
Y. Manetas ◽  
N. A. Gavalas
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Carboxylase Activity ◽  
Maize Leaf

scholarly journals Relationship between NH+4 Assimilation Rate and in Vivo Phosphoenolpyruvate Carboxylase Activity

1990 ◽  
Vol 94 (1) ◽  
pp. 284-290 ◽  
Author(s):  
Greg C. Vanlerberghe ◽  
Kathryn A. Schuller ◽  
Ronald G. Smith ◽  
Regina Feil ◽  
William C. Plaxton ◽  
...  
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Assimilation Rate ◽  
Carboxylase Activity

scholarly journals A study of stabilization of gluconeogenic activity in rat liver slices by calcium and manganese ions

1972 ◽  
Vol 129 (2) ◽  
pp. 231-239 ◽  
Author(s):  
Anne Roobol ◽  
G. A. O. Alleyne
Keyword(s):  
Rat Liver ◽  
Phosphoenolpyruvate Carboxylase ◽  
Incubation Medium ◽  
Lysosomal Enzymes ◽  
Glucose Production ◽  
Liver Slice ◽  
Manganese Ions ◽  
Slice Preparation ◽  
Carboxylase Activity ◽  
Bivalent Cations

1. The effect of some bivalent cations on gluconeogenesis by the rat liver-slice preparation has been investigated. 2. Ca2+and Mn2+stimulated glucose production from a range of substrates but not from glycerol. Mg2+had no effect on the rate of glucose production. 3. Ca2+were required to maintain phosphoenolpyruvate carboxylase activity in the slice preparation. 4. Ca2+and Mn2+, but not Mg2+, retarded the release of lysosomal enzymes from the slice into the incubation medium. 5. It is proposed that Ca2+and Mn2+stimulate glucose production by stabilizing the lysosome system in the liver-slice preparation. 6. The value of the liver-slice preparation as a means of measuring hepatic gluconeogenesis is discussed.

scholarly journals Carboxylation and dephosphorylation of phosphoenol-3-fluoropyruvate by maize leaf phosphoenolpyruvate carboxylase

1988 ◽  
Vol 253 (1) ◽  
pp. 217-222 ◽  
Author(s):  
D H Gonzalez ◽  
C S Andreo
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Maize Leaf ◽  
Propenoic Acid

The analogue (Z)-phosphoenol-3-fluoropyruvate [(Z)-3-fluoro-2-(phosphono-oxy)propenoic acid] was tested as substrate of maize leaf phosphoenolpyruvate carboxylase. Studies with NaH14CO3 indicate that the analogue is carboxylated by the enzyme. However, this reaction accounts for only one-tenth of the activity measured by Pi liberation. The rest of the analogue is merely dephosphorylated. This is the first analogue for which both carboxylation and dephosphorylation have been observed.

Stability Studies on Maize Leaf Phosphoenolpyruvate Carboxylase: The Effect of Salts

Biochemistry ◽  
1995 ◽  
Vol 34 (2) ◽  
pp. 472-480 ◽  
Author(s):  
Wayne A. Jensen ◽  
John McD. Armstrong ◽  
Joe DeGiorgio ◽  
Milton T. W. Hearn
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Stability Studies ◽  
Maize Leaf
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