Journal article

Solubilization, purification and kinetic properties of three membrane-bound long-chain acyl-coenzyme-A thioesterases from microsomes of photosynthetic tissue.

DJ Murphy, KD Mukherjee, E Latzko, IE Woodrow

Eur J Biochem | Published : 1984


Microsomal membranes of developing pea (Pisum sativum) leaves contained almost one third of the total long-chain acyl-CoA thioesterase activity found in the leaf cell. Three distinct forms of long-chain acyl-CoA thioesterase were purified by a combination of cholate-solubilization, dialysis, ion-exchange, and gel-filtration chromatography. Purification factors of 4600, 100 and 280 were achieved for the thioesterase forms I, II and III, respectively. Apparent molecular masses were: form I, 28 kDa; form II, 140 kDa; form III, 139 kDa. All the three thioesterases showed overlapping specificities towards palmitoyl-CoA, stearoyl-CoA, and oleoyl-CoA but were inactive towards short-chain acyl-CoAs,..

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University of Melbourne Researchers