The role of galactolipids in spinach chloroplast lamellar membranes: I. Partial purification of a bean leaf galactolipid lipase and its action on subchloroplast particles.

A galactolipid lipase has been isolated and partially purified from the chloroplast fraction of the primary leaves of Phaseolus vulgaris var. Kentucky Wonder. The lipase hydrolyzed monogalactosyl diglyceride rapidly and phosphatidyl choline relatively slowly. Triolein and p-nitrophenyl stearate were not hydrolyzed.Spinach subchloroplast particles were excellent substrates for the lipase. Initial rates of fatty acid release from subchloroplast particles at 30 C by the lipase as high as 60 microequivalents per minute per milligram protein were observed. At completion of the reaction, about 2.7 microequivalents of fatty acid were liberated per milligram of chlorophyll in the subchloroplast particles, indicating that major amounts of lipid in the particles were rapidly attacked by the lipase.The treatment of subchloroplast particles with the lipase resulted in a rapid inhibition of light-dependent electron flow. This inhibition was largely prevented when the incubation was carried out in the presence of high concentrations of defatted bovine serum albumin. These results suggest that when precautions are taken to prevent the binding of fatty acids to the subchloroplast particles, large amounts of lipid may be removed without a marked effect on electron flow.