Purification and partial characterization of a bacterial phospholipid: cholesterol acyltransferase.

摘要: Abstract A glycerophospholipid:cholesterol acyltransferase has been purified to near homogeneity from cell-free culture supernatants of Aeromonas salmonicida. The characteristics the enzyme distinguish it bacterial phospholipases; however, shares several properties with lecithin:cholesterol mammalian plasma. Thus, inhibits 2-positional specificity as an and will act a phospholipase A2 in absence cholesterol. Furthermore, no divalent cation requirement is stimulated both by albumin human apolipoprotein A-I. Unlike acyltransferase, not specific for phosphatidylcholine addition can use erythrocyte membranes substrates. Similar Naja naja A2, acts asymmetrically on intact erythrocytes.