scholarly journals The localization of adenosine triphosphatases in morphologically characterized subcellular fractions of guinea-pig brain

1965 ◽  
Vol 96 (2) ◽  
pp. 404-412 ◽  
Author(s):  
RJA Hosie
Keyword(s):  
Guinea Pig ◽  
Subcellular Fractions ◽  
Pig Brain ◽  
Adenosine Triphosphatases ◽  
Guinea Pig Brain

scholarly journals The subcellular distribution of triphosphoinositide phosphomonoesterase in guinea-pig brain

1972 ◽  
Vol 128 (3) ◽  
pp. 579-586 ◽  
Author(s):  
A. Sheltawy ◽  
M. Brammer ◽  
D. Borrill
Keyword(s):  
Guinea Pig ◽  
Subcellular Fractions ◽  
Assay System ◽  
Acid Phosphatases ◽  
Alkaline Phosphatases ◽  
Pig Brain ◽  
Optimum Ph ◽  
Ph Range ◽  
Guinea Pig Brain ◽  
Optimum Ph Range

1. Some properties of the triphosphoinositide phosphomonoesterase from the homogenates of guinea-pig brain were studied. The enzyme has an optimum pH range 6.7–7.3, is stimulated with KCl at a concentration of 0.1m, and under these conditions has Km1.43×10-4m. 2. A factor from the ‘pH5 supernatant’ of guinea-pig brain stimulates the enzyme activity over and above the stimulation produced by KCl. Subcellular fractions of guinea-pig brain varied in their response to the ‘pH5 supernatant’. Maximum stimulation was observed with the P1 fraction, containing myelin and nuclei. 3. An assay system for the enzyme was developed that contained optimum concentrations of both KCl and the ‘pH5 supernatant’. Acid phosphatases were inhibited by NaF, but, in contrast with previous work, no EDTA was added to the assay system to inhibit the alkaline phosphatases. This reagent inhibited the triphosphoinositide phosphomonoesterase. It was estimated that the remaining fraction of non-specific phosphatases can account for only 14% of the observed triphosphoinositide phosphomonoesterase activity. 4. Subcellular fractions of guinea-pig brain were characterized by electron microscopy and subcellular markers. The triphosphoinositide phosphomonoesterase exhibited a distribution between the fractions similar to that of 5′-nucleotidase, but different from that of alkaline phosphatase.

ENZYME ACTIVITIES OF THE SUBCELLULAR FRACTIONS OF MYELIN IN THE DEVELOPING GUINEA-PIG BRAIN

2009 ◽  
Vol 46 (S43) ◽  
pp. 231-231
Author(s):  
H. Frey ◽  
P. Riekkinen ◽  
A. Arstila ◽  
U. K. Rinne
Keyword(s):  
Guinea Pig ◽  
Enzyme Activities ◽  
Subcellular Fractions ◽  
Pig Brain ◽  
Guinea Pig Brain
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