Cholinergic modulation of baker’s yeast cell phagocytosis by rat astrocytes

2004 ◽  
Vol 365 (1) ◽  
pp. 19-22 ◽  
Author(s):  
Ricardo M Gómez ◽  
Marı́a I Berrı́a ◽  
Leonor Sterin-Borda
2021 ◽  
Vol 19 (6) ◽  
pp. 49-53
Author(s):  
Tatyana Vasilyevna Ryabtseva ◽  
Denis Alexandrovich Makarevich ◽  
Evgeny Mikhailovich Ermola

1969 ◽  
Vol 112 (5) ◽  
pp. 747-754 ◽  
Author(s):  
J. J. Cazzulo ◽  
A. O. M. Stoppani

1. Pyruvate carboxylase from baker's yeast acts with either MgATP2− or MnATP2− as substrate. The optimum pH for the enzyme reaction is 8·0 with MgATP2− and 7·0 with MnATP2−. 2. When the reaction velocity is plotted against MgATP2− (or MnATP2−) concentration slightly sigmoid curves are obtained, either in the presence or in the absence of acetyl-CoA (an allosteric activator). In the presence of excess of free Mg2+ (or Mn2+) the curves turn into hyperbolae, whereas in the presence of excess of free ATP4− the apparent sigmoidicity of the curves increases. 3. The sigmoidicity of the plots of v against MgATP2− (or MnATP2−) concentration can be explained by the inhibitory effect of free ATP4−, the concentration of which, in the experimental conditions employed, is significant and varies according to the total concentration of the ATP–magnesium chloride (or ATP–manganese chloride) mixture. Free ATP4− behaves as a negative modifier of yeast pyruvate carboxylase. 4. The effect of high concentrations of Mg2+ (or Mn2+) on the kinetics of yeast pyruvate carboxylase can be explained as a deinhibition with respect to ATP4−, instead of a direct enzyme activation. 5. At pH6·5 manganese chloride is more effective than magnesium chloride as enzyme activator even in the presence of a great excess (16-fold) of the latter. This is consistent with a significant contribution of the MnATP2− complex to the activity of yeast pyruvate carboxylase, in medium conditions resembling those existing inside the yeast cell (pH6·25–6·75; 12mm-magnesium chloride and 0·75mm-manganese chloride). 6. The physiological significance of the enzyme inhibition by free ATP4− is doubtful since the Mg2+ and Mn2+ concentrations reported to exist inside the yeast cell are sufficient to decrease ATP4− concentrations to ineffective values.


2014 ◽  
Vol 163 ◽  
pp. 108-113 ◽  
Author(s):  
Chema Borchani ◽  
Fabienne Fonteyn ◽  
Guilhem Jamin ◽  
Michel Paquot ◽  
Christophe Blecker ◽  
...  

1978 ◽  
Vol 84 (1) ◽  
pp. 5-8 ◽  
Author(s):  
Elke Parkkinen ◽  
Erkki Oura ◽  
Heikki Suomalainen

2014 ◽  
Vol 13 (12) ◽  
pp. 3153-3160 ◽  
Author(s):  
Zakaria Al-Qodah ◽  
Mohammad Al-Shannag ◽  
Kholoud Alananbeh ◽  
Nahla Bouqellah ◽  
Eman Assirey ◽  
...  

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