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ENZYMATIC ACYLATION OF 1‐ALKYL‐, 1‐ALKENYL‐AND 1‐ACYL GLYCERO‐3‐PHOSPHORYLETHANOLAMINE IN DEVELOPING RAT BRAIN
Author(s) -
Natarajan V.,
Sastry P. S.
Publication year - 1974
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1974.tb06933.x
Subject(s) - microsome , acylation , alkyl , chemistry , enzyme , transferase , biochemistry , acyl group , acyl coa , mitochondrion , stereochemistry , organic chemistry , catalysis
— Rat brain particulate fractions were shown to acylate [ 32 P]1‐alkyl‐ sn ‐glycero‐3‐phosphorylethanolamine (GPE). While the main product is 1‐alkyl‐2‐acyl GPE, about 12 per cent of the radioactivity was also found in 1‐alkenyl‐2‐acyl GPE. The acyl transferase activity was completely dependent on added ATP and CoA and it was localized mainly in the microsomal fraction. A comparative study of acyl transferase activities to 1‐alkyl‐, 1‐alkenyl‐, and 1‐acyl GPE by crude mitochondrial fraction and microsomes of 10, 16 and 22‐day‐old rat brains showed a progressive increase in activity with development. In the 22‐day‐old rat brain the order of activity towards the three substrates is as follows: 1‐acyl GPE ± 1‐alkenyl GPE ± 1‐alkyl GPE with a crude mitochondrial fraction and 1‐acyl GPE ± 1‐alkyl GPE ± 1‐alkenyl GPE with microsomes.