Premium
Acid phosphatase activity in the isolated brush border membrane of the tapeworm, Hymenolepis diminuta : Partial, characterization and differentiation from the alkaline phosphatase activity
Author(s) -
Pappas Peter W.
Publication year - 1988
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240370407
Subject(s) - alkaline phosphatase , hymenolepis diminuta , acid phosphatase , chemistry , phosphatase , phosphate , biochemistry , brush border , sodium orthovanadate , membrane , hydrolysis , enzyme , biology , vesicle , cestode infections , helminths , zoology
The isolated brush border membrane of the tapeworm, Hymenolepis diminuta , hy‐drolyzes p‐nitrophenyl phosphate over a broad pH range. Acid phosphatasc activity (pH optimum at 4.0) is inhibited specifically by sodium dodecyl sulfate (SDS) and NaF, while the alkaline phosphatase activity (pH optimum at 8.8) is inhibited specifically by levamisole, 2‐mercaptoethanol, and ethylenediaminetetra‐acetate (EDTA). These two phosphatase activities are further differentiated in that (1) there is a rapid decrease in alkaline phosphatase activity when the membrane preparation is incubated at pH 4.0, while there is little loss of acid phosphatase activity, and (2) the alkaline phosphatase activity is solubilized with no loss of activity when the membrane is treated with Triton X‐100, while such treatment causes a significant loss of acid phosphalase activity. Both activities are nonspecific and hydrolyze a variety of phos‐phorylated compounds, but the relative activities of the two phosphatases against these substrates vary significantly.