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Last Updated: 3 years ago

Possible Interaction: Adenosine Triphosphate and Glycerol

Research Papers that Mention the Interaction

In the absence of acetylglutamate, glycerol (an effective activator) reduces the Km's for ATP and K+, increases the Vmax, and dramatically reduces the S0.5 for acetylglutamate to <1 μM for the synthetase reaction.
In the presence of excess acetylglutamate, glycerol markedly reduces the Km for ATP for the synthetase, decreases the Vmax, NH4+ becomes a more effective activator than K+, and Na+ activates appreciably.
Molecular and Cellular Biochemistry  •  2004  |  View Paper
Glycerol barely affected the TF spectra of all GKs but decreased k(cat), glucose S(0.5) and K(D) values and ATP K(M) while leaving cooperativity unchanged.
Biochimica et biophysica acta  •  2012  |  View Paper
It appears that HAES, but not glycerol , significantly reduces ATP concentrations whereas both lead to a reduction of 2,3‐DPG concentrations; this reduction was more pronounced with glycerol than with HAES.
Vox sanguinis  •  1992  |  View Paper
The results indicate that glycerol lowered the rate of ATP generation of platelets stored at 22 degrees C. However, the removal of glycerol reversed the decreased energy metabolism.
Cryobiology  •  1988  |  View Paper
When 1mM ATP is added to human dermal fibroblasts (DF) in monolayer culture permeabilized by glycerol , they undergo a rapid reduction in length and their intracellular actin filaments aggregate.
Journal of cellular physiology  •  1986  |  View Paper
Stuclies have been made of a number of factors which might influence the amount of tension generated in glycerinated myocardial fibers by ATP.
The Journal of pharmacology and experimental therapeutics  •  1958  |  View Paper
Moreover, addition of glycerol protected glycolysis, ATP levels, phosphorylation of PKA substrates and PTP against the influence of SACH.
PloS one  •  2012  |  View Paper
Isolated tissue permeabilized with Triton X‐100 or glycerol reversibly contracted in the presence of ATP.
The Journal of comparative neurology  •  2003  |  View Paper
The ATP hydrolysing activity of the enzyme decreased differently on adding sucrose and glycerol.
Biochimica et biophysica acta  •  1997  |  View Paper
In the … 50% glycerol , the inactivation parameters were somewhat altered (k(inact) = 0.3 …(-3) s-1 and K(inact) = 0.2 mM); ATP Mg2+ proved to afford a mixed competitive-non competitive protection effect, while histone … in a competitive manner with a Kp of 0.06 microgram/ml.
Biochimie  •  1993  |  View Paper
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