The binding of human lysosomal elastase to glomerular basement membrane.
The interaction of purified elastase with glomerular basement membrane and its antigens was studied. There appears to be at least two types of interaction. The first is a weak interaction and the enzyme can be removed simply by extended washing with neutral buffer. The second, stronger interaction is desorbed with high salt concentration at alkaline pH. The different interactions probably represent the binding of isoenzymes. Further experiments demonstrate that all isoenzymes degrade the membrane. Serum proteins prevent binding and inhibit the action of elastase on glomerular basement membrane.
D001485:Basement Membrane / Q000276:immunology / Q000378:metabolism*; D002021:Buffers; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000378:metabolism; D007678:Kidney Glomerulus / Q000378:metabolism*; D008247:Lysosomes / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000378:metabolism*; D011485:Protein Binding
D002021:Buffers; D007527:Isoenzymes; D010196:Pancreatic Elastase