Purification and characterization of an acid phosphatase from Arachis hypogaea.
An acid phosphatase from Arachis hypogaea (peanuts) has been purified. The electrophoretically homogeneous enzyme preparation is free of any phophodiesterase activity. The enzyme has a molecular weight of 120,000. Among the various phosphomonoesters tested, p-nitrophenylphosphate was found to be its most effective substrate. The Km for p-nitrophenylphosphate was 1.21 mM at pH 5.0 and 25 degrees C. The enzyme was thermostable and did not loose activity after 1 hr at 50 degrees C.
Srivastava
R
R
Chemistry Department I.I.T. Delhi, India.
Rajput
Y S
YS
Khare
S K
SK
Tyagi
R
R
Gupta
M N
MN
D000135:Acid Phosphatase / Q000737:chemistry / Q000302:isolation & purification* / Q000502:physiology; D010367:Arachis / Q000737:chemistry / Q000201:enzymology*; D005591:Chemical Fractionation; D002845:Chromatography / Q000379:methods; D002850:Chromatography, Gel / Q000379:methods; D004586:Electrophoresis; D005459:Fluorides / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D009596:Nitrophenols / Q000378:metabolism; D009943:Organophosphorus Compounds / Q000378:metabolism; D013379:Substrate Specificity
D009596:Nitrophenols; D009943:Organophosphorus Compounds; C008644:nitrophenylphosphate; D000135:Acid Phosphatase; D005459:Fluorides