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Enzymic synthesis of 1‐alkyl‐2‐acyl‐ sn ‐glycero‐3‐phosphorylethanolamine through ethanolaminephosphotransferase activity in the neuronal and glial cells of rabbit in vitro
Author(s) -
Roberti R.,
Binaglia L.,
Francescangeli E.,
Goracci G.,
Porcellati G.
Publication year - 1975
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02534148
Subject(s) - chemistry , biochemistry , in vitro , alkyl , ethanolamine , incubation , stereochemistry , organic chemistry
The transfer of radioactivity from cytidine‐5′‐diphosphate ethanolamine into 1‐alkyl‐2‐acyl‐ sn ‐glycerophosphorylethanolamine of neuronal and glial cells from adult rabbit brain cortex has been investigated in vitro. The synthesis of 1‐alkyl‐2‐acyl‐ sn ‐glycerophosphorylethanolamine in both cell populations was stimulated 23–25‐fold by the addition of 6 mM alkylacylglycerol. The neuronal cell‐enriched fraction was found to possess/unit protein a 1.7–1.8‐fold ethanolaminephosphotransferase activity (EC 2.7.8.1), as compared to the glial fraction, when saturating concentrations (6 mM) of alkylacylglycerols were added in the incubation system. The neuronal/glial ratio was 2.6–2.8 in the absence of lipid acceptor or with low concentrations of alkylacylglycerol. Under most favorable conditions, 6.4 and 3.3. nmoles 1‐alkyl‐2‐acyl‐ sn ‐glycerophosphorylethanol‐amine/mg protein/30 min was obtained for neurons and glia, respectively. Various kinetic properties of the 1‐alkyl‐2‐acyl‐ sn ‐glycerophosphorylethanolamine synthesizing phosphotransferase activity were found to be similar both in neurons and glia.