Heparan sulphate and the binding of lipoprotein lipase to porcine thoracic aorta endothelium |
| |
Authors: | Monica P Williams Heather B Streeter Frederick S Wusteman Anthony Cryer |
| |
Institution: | Department of Biochemistry, University College, P.O. Box 78, Cardiff CF 1 1XL U.K. |
| |
Abstract: | Purified bovine milk lipoprotein lipase was shown to bind to intact porcine aortic endothelium in a specific, saturable fashion. The binding was reversed by exogenous heparin. A single class of binding sites was involved and at saturation 1.24?1011 molecules of lipoprotein lipase / cm2 were bound. This represents 0.51?106 enzyme molecules per endothelial cell at a density of 1.2?103 molecules / μm2. The enzyme binding was reduced by prior trypsinisation of the endothelial surface under conditions that removed cell surface glycosaminoglycan chains. The porcine endothelium was shown to have available at its surface 5.4?1011 chains of heparan sulphate plus heparin-like glycosaminoglycans / cm2. Such as excess suggests that lipoprotein lipase may interact with approximately one in four of the available heparan sulphate chains. |
| |
Keywords: | Heparan sulfate Lipoprotein lipase Membrane-enzyme interaction (Pig thoracic aorta) |
本文献已被 ScienceDirect 等数据库收录! |