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- W2171457319 abstract "Abstract The high M , acid phosphatase (EC 3.1.3.2) from barley ( Hordeum vulgare ) coleoptiles was purified 57-fold by ammonium sulphate fractionation, DEAE-cellulose, Con A-Sepharose 4B and gel filtration chromatography. The molecular weight of the native enzyme was 104 000 and 106 000 measured by gel filtration on a Sephadex G-100 column and by density gradient ultracentrifugation, respectively. The enzyme is a heterodymer and consists of two subunits of 79 400 and 26 000 as determined by SDS-PAGE. The apparent K m value with p -nitrophenyl phosphate ( p NPP) as substrate was 0.10 mM. The enzyme activity was unaffected by phosphate acceptors such as glycerol, methanol, ethanol and glucose, but was strongly inhibited by Hg 2+ , Cu 2+ , molybdate ion and NaF. The acid phosphatase from barley coleoptiles hydrolysed a wide variety of phosphate esters and the highest activity was observed with ATP, inorganic pyrophosphate, p NPP and ADP." @default.
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- W2171457319 date "1992-01-01" @default.
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- W2171457319 title "High molecular weight acid phosphatase from barley coleoptiles" @default.
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- W2171457319 doi "https://doi.org/10.1016/s0031-9422(00)97512-5" @default.
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