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Solubilization of membrane-bound ribonuclease (RNAse) and alkaline phosphatase from the isolated brush border of Hymenolepis diminuta (Cestoda)



Solubilization of membrane-bound ribonuclease (RNAse) and alkaline phosphatase from the isolated brush border of Hymenolepis diminuta (Cestoda)



Journal of Parasitology 66(3): 434-438



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.

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Accession: 021766177

Download citation: RISBibTeXText

PMID: 7391887

DOI: 10.2307/3280744



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