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Lung lamellar bodies lack certain key enzymes of phospholipid metabolism
Author(s) -
Garcia Agustina,
Sener Stephen F.,
Mavis Richard D.
Publication year - 1976
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/bf02532659
Subject(s) - lamellar granule , biochemistry , acyltransferase , enzyme , microsome , phospholipid , chemistry , pulmonary surfactant , acyltransferases , organelle , biology , biosynthesis , membrane
Palmitoyl CoA‐glycerol‐3‐phosphate acyltransferase, phosphatidate phosphohydrolase, and phospholipase A were assayed in subcellular fractions of rat lung, including lamellar bodies, the putative site of storage and secretion of lung surfactant. The specific activity of each of these enzymes in lamellar bodies was relatively low and could be entirely accounted for by a small contamination of the lamellar bodies fraction by microsomes, as quantitated by the presence of the microsomal marker reduced triphosphopyridine nucleotide cytochrome c reductase. These data indicate that lamellar bodies are not the site of synthesis of the lipid component of pulmonary surfactant by pathways involving these enzymes.