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. 1984 May 1;219(3):781–784. doi: 10.1042/bj2190781

Phospholipid substrate-specificity of the L-serine base-exchange enzyme in rat liver microsomal fraction.

K S Bjerve
PMCID: PMC1153544  PMID: 6430274

Abstract

The specificity of the L-serine base-exchange enzyme towards the fatty acid composition of the phospholipid substrate was investigated with a rat liver microsomal fraction. The relative rates of L-serine incorporation into saturated-hexaenoic, saturated-pentaenoic, saturated-tetraenoic, saturated-trienoic, dienoic-dienoic, monoenoic-dienoic, saturated-dienoic and saturated-monoenoic + saturated-saturated phosphatidylserine molecular species were 42, 5, 23, 4, 5, 4, 5 and 11% respectively. This is similar to, but not identical with, the relative mass abundance of these molecular species in total liver cell phosphatidylserines. The results indicate that the substrate-specificity of the L-serine base-exchange enzyme can at least in part explain the observed fatty acid composition of rat liver phosphatidylserines.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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