On the specificity of rat-liver lysophospholipase
Publication date
1968-10-22
Authors
Bosch, H. van den
Aarsman, A.J.
Slotboom, A.J.
Deenen, L.L.M. van
Editors
Advisors
Supervisors
DOI
Document Type
Article
Metadata
Show full item recordCollections
License
Abstract
1. 1. A study on the specificity of rat-liver lysophospholipase activity (EC 3.1.1.5) revealed that both 1-acyl-sn-glycero-3-phosphorylcholine and 2-acyl-sn-glycero-3-phosphorylcholine are deacylated. From both positional isomers the unsaturated analogs appeared to be degraded at higher rates.
2. 2. Circumstantial evidence is presented indicating that 2-acyl-sn-glycero-3-phosphorylcholine can be attacked directly by this lysophospholipase activity without a prior migration of the fatty acyl constituent.
3. 3. Compounds lacking the free hydroxyl group present in lysophosphatidyl-cholines, e.g. acyl-ethylene glycolphosphorylcholine and 1-acyl-propane diol-3-phosphorylcholine, also fall in the enzyme's range of specificity.
4. 4. Mono-acyl derivatives of sn-glycero-1-phosphorylcholine, sn-glycero-2-phosphorylcholine, as well as sn-glycero-3-phosphorylcholine, were found to be degraded.
5. 5. Inhibition of lysophospholipase activity by various agents exhibited the same effect on the deacylation of both 1-acyl- and 2-acyl-sn-glycero-3-phosphoryl-choline.
6. 6. The degradation of mono-acyl-phosphatidylcholine appeared to be strongly inhibited in the presence of phosphatidylcholine.