The effect of membrane phospholipid acyl-chain composition on the activity of brain-beta-N-acetyl-D-glucosaminidase

The phospholipid acyl-chain dependence of the membrane-bound lysosomal beta-N-acetyl-D-glucosaminidase has been examined on control membranes from rat brain primary cell cultures and on membrane modified by culturing the cells in media supplemented with polyunsaturated fatty acids. The relationship...

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Bibliographic Details
Published in:Biochemical journal 1981-05, Vol.195 (2), p.383-388
Main Authors: Orlacchio, A, Maffei, C, Binaglia, L, Porcellati, G
Format: Article
Language:English
Subjects:
Acetylglucosaminidase - metabolism
Animals
Brain - enzymology
Cells, Cultured
Chemical Phenomena
Chemistry
Enzyme Activation - drug effects
Hexosaminidases - metabolism
Lysosomes - enzymology
Membrane Lipids - pharmacology
Phosphatidylcholines - pharmacology
Phosphatidylethanolamines - pharmacology
Phospholipids - pharmacology
Rats
Subcellular Fractions - enzymology
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Summary:The phospholipid acyl-chain dependence of the membrane-bound lysosomal beta-N-acetyl-D-glucosaminidase has been examined on control membranes from rat brain primary cell cultures and on membrane modified by culturing the cells in media supplemented with polyunsaturated fatty acids. The relationship between beta-N-acetyl-D-glucosaminidase activity and the membrane phospholipid acyl-chain composition has been evaluated. An increase in the unsaturation level of phosphatidyl ethanolamines and phosphatidylcholines, the most abundant phospholipids in this membrane fraction, is related to the rate of the enzymic reaction. The Arrhenius plot of the enzyme activity in modified membranes shows break-temperatures, starting from approximately 15 degrees C. The apparent activation energy below and above the break-temperature is not correlated with phospholipid acyl-chain unsaturation.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj1950383