Solubilization of membrane-bound ribonuclease (RNAse) and alkaline phosphatase from the isolated brush border of Hymenolepis diminuta (Cestoda).
Plasma membrane from the brush border isolated from the tegument of Hymenolepis diminuta contains membrane-bound ribonuclease (RNase) and alkaline phosphatase activities. RNase (yeast RNA substrate), alkaline phosphatase (p-nitrophenyl phosphate substrate), and additional membrane proteins were solubilized by sonication or treatment with the detergents dodecyl trimethylammonium bromide, beta-octyl-D-glucopyranoside, sodium dodecyl sulfate (SDS), or ZwittergentTM 3-12 (N-dodecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate). At optimal conditions, greater than 90% of both enzymes and total protein were solubilized by the latter two detergents, whereas beta-octyl-D-glucopyranoside, dodecyl trimethylammonium bromide, and sonication were only partially effective. Nonionic detergents did not solubilize the membrane effectively.
D000469:Alkaline Phosphatase / Q000302:isolation & purification*; D000818:Animals; D002458:Cell Fractionation; D002462:Cell Membrane / Q000201:enzymology*; D003902:Detergents / Q000494:pharmacology; D006926:Hymenolepis / Q000201:enzymology* / Q000648:ultrastructure; D008871:Microvilli / Q000201:enzymology*; D012260:Ribonucleases / Q000302:isolation & purification*; D012995:Solubility; D013010:Sonication; D013696:Temperature
D003902:Detergents; D012260:Ribonucleases; D000469:Alkaline Phosphatase