Abstract
AbstractStearyl‐CoA, oleyl‐CoA and elaidyl‐CoA were prepared and tested as substances in synthesizing lecithin from 1‐ and 2‐acyglycerol‐3‐phosphorylcholine. The rates of acyltransfer were followed by a continuous spectrophotometric assay. The enzyme(s) used to catalyze esterification at the 2‐position did not discriminate appreciably between thecis andtrans isomers of octadecenoate and transferred them more rapidly than the saturated acid, octadecanoate. However, the enzyme(s) which acted at the 1‐position discriminated markedly between the geometric isomers and rapidly transferred totrans‐ octadecenoate and octadecanoate.
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