Clinical Chemistry
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Clinical Chemistry 33: 81-86, 1987;
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Clinical Chemistry, Vol 33, 81-86, Copyright © 1987 by American Association for Clinical Chemistry

Automated enzymatic measurement of lecithin, sphingomyelin, and phosphatidylglycerol in amniotic fluid

CA Bradley, KE Salhany, SS Entman, SL Aleshire and FF Parl

We describe methods for automated enzymatic measurement of lecithin, sphingomyelin, and phosphatidylglycerol in amniotic fluid. Phospholipase C (EC 3.1.4.3) and sphingomyelin phosphodiesterase (EC 3.1.4.12) are reacted with lecithin and sphingomyelin, respectively, to liberate phosphocholine. Phosphocholine is then reacted with alkaline phosphatase, choline oxidase, peroxidase, and 4-aminoantipyrine to form a colored complex, for which the absorbance at 500 nm is measured with a centrifugal analyzer. Phosphatidylglycerol is hydrolyzed by phospholipase D (EC 3.1.4.4) to form glycerol, which is subsequently reacted with ATP and NAD+ in the presence of glycerol kinase and glycerol-3-phosphate dehydrogenase to yield NADH. The absorbance of the NADH formed is measured at 340 nm. These methods provide a simple, rapid, and accurate alternative to thin-layer chromatography for determination of phospholipids in amniotic fluid for assessment of fetal lung maturity.


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K.-A. Rye, N. J. Hime, and P. J. Barter
The Influence of Sphingomyelin on the Structure and Function of Reconstituted High Density Lipoproteins
J. Biol. Chem., February 23, 1996; 271(8): 4243 - 4250.
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Copyright © 1987 by the American Association for Clinical Chemistry.