Kidney microvillus peptidases--are they transmembrane proteins?
The membrane of kidney microvilli is richly endowed with peptidases. Present information is that there are at least eight examples located in this membrane. Three of the group are known to be among the major proteins that can be identified by dodecyl sulphate electrophoresis of the purified microvillus fraction. These three peptidases, aminopeptidase M, serine peptidase (dipeptidyl peptidase IV) and neutral endopeptidase can be labelled by lactoperoxidase iodination from either the luminal or the inner surfaces of the membrane, a result consistent with the view that the polypeptide chains span the microvillus membrane. The serine peptidase has been purified by two methods, permitting a comparison of the detergent-released and proteinase-released forms. The two forms differ in the presence and absence of the hydrophobic anchor that secures the enzyme to the membrane. Preliminary studies support the view that this hydrophobic domain is relatively small and that it includes the N-terminal region of the polypeptide chain.
D000409:Alanine; D000626:Aminopeptidases / Q000378:metabolism; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology*; D004151:Dipeptides; D010450:Endopeptidases / Q000378:metabolism; D007687:Kidney Tubules, Proximal / Q000201:enzymology* / Q000648:ultrastructure; D008871:Microvilli / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity; D013552:Swine
D004151:Dipeptides; D010450:Endopeptidases; D010447:Peptide Hydrolases; D000626:Aminopeptidases; D000409:Alanine