|
KMID : 1007519940030010029
|
|
Food Science and Biotechnology
1994 Volume.3 No. 1 p.29 ~ p.33
|
|
|
Properties of Acid Phosphatase from Pear
|
|
Shin, Mi-Hae
Yoon, Yur-Yang/Kim, Gi-Nahm/Kil, Ji-Eun/Park, Inshik
|
|
|
Abstract
|
|
|
|
Acid phosphatase from pear has been partially purified by ammonium sulfate fractionation, Sephacry1 S-200 gel filtration, CM-Sepharose CL-6B, and DEAE-Sephacel ion exchange chromatography. The optimum pH and temperature for the enzyine reaction with p-nitropheny1 phosphate as a substrate were pH 5.5 and 55℃, respectively. The enzyme was most stable at pH 7,0. The preferred substrate for the enzyme was identified as p-nitropheny1 phosphate, while 5´-GMP and 5´IMP were poor substrates for the enzyme. The Michaelis-Menten constant of the enzyme with p-nitropheny1 phosphate was 1.53 mM. The enzyme activity was inhibited by molybdate, metavanadate, fluoride ions and L-phenylalanine.
|
|
|
KEYWORD
|
|
|
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
 
|
|