title: Release of GPI-anchored membrane aminopeptidase P by enzymes and detergents has some peculiarities.
abstract: The enzyme aminopeptidase P (APP) of rat small intestine is an integral membrane protein. It is not released from the membrane by proteinases and is also resistant to bacterial inositol-specific phospholipases C (PI-PLC's). We show that this resistance is due to a hindered accessibility of the bond split by PI-PLC and not to a modified glycosylphosphatidyl inositol (GPI)-anchor.
authors.affiliation: Institute of Physiological Chemistry, Medical Faculty, Martin-Luther-University, Halle/Saale, Germany.
authors.forename: R
authors.initials: R
authors.lastname: Koelsch
authors.forename: S
authors.initials: S
authors.lastname: Gottwald
authors.forename: J
authors.initials: J
authors.lastname: Lasch
mesh_terms: D000626:Aminopeptidases / Q000737:chemistry*; D000818:Animals; D002462:Cell Membrane / Q000737:chemistry; D003902:Detergents / Q000494:pharmacology*; D017261:Glycosylphosphatidylinositols / Q000737:chemistry*; D007421:Intestine, Small / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology*; D008871:Microvilli / Q000737:chemistry; D051381:Rats; D010738:Type C Phospholipases / Q000494:pharmacology*
chemical_list: D003902:Detergents; D017261:Glycosylphosphatidylinositols; D010738:Type C Phospholipases; D000626:Aminopeptidases; C022750:X-Pro aminopeptidase