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Lung surfactant synthesis: a Ca++-dependent microsomal phospholipase A2 in the lung.
Authors:A Garcia  J D Newkirk  R D Mavis
Institution:Department of Biochemistry, Northwestern University Dental & Medical Schools, Chicago, Illinois 60611 USA
Abstract:We present the first direct evidence for a highly active, Ca++-dependent phospholipase A2 in the microsomal fraction of rat lung homogenate. Several previously reported studies from other laboratories strongly implicate this enzyme as a key metabolic step in the biosynthesis of dipalmitoyl lecithin, the primary component of pulmonary surfactant. In the present study, stoichiometric amounts of 3H]lysophosphatidylethanolamine and 14C]fatty acid were released during incubation of 1-9, 10-3H]palmitoyl-2-sn-1′-14C]linoleoyl phosphatidylethanolamine with the lung microsomal fraction. Marker enzyme measurements showed that the microsomal activity cannot be due to contamination with mitochondria, which also show phospholipase A2 in both lung and liver. In contrast, liver microsomes show predominantly a phospholipase A1 activity.
Keywords:PE  phosphatidylethanolamine  LPE  lysophosphatidylethanolamine  FA  fatty acid  BSA  bovine serum albumin  PPO  2  5-diphenyloxazole
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