Purification and properties of a glycerophosphocholine phosphodiesterase from bovine brain myelin

1994 ◽  
Vol 19 (1) ◽  
pp. 43-48 ◽  
Author(s):  
Jun Yuan ◽  
J. N. Kanfer
Keyword(s):  
Bovine Brain ◽  
Purification And Properties ◽  
Glycerophosphocholine Phosphodiesterase

Purification and Properties of Pyridoxal Kinase from Bovine Brain

1993 ◽  
pp. 203-207
Author(s):  
Tae Hirakawa-Sakurai ◽  
Kiyoshi Ohkawa ◽  
Makoto Matsuda
Keyword(s):  
Bovine Brain ◽  
Pyridoxal Kinase ◽  
Purification And Properties

scholarly journals Purification and properties of myo-inositol-1-phosphatase from bovine brain

1988 ◽  
Vol 253 (2) ◽  
pp. 387-394 ◽  
Author(s):  
P V Attwood ◽  
J B Ducep ◽  
M C Chanal
Keyword(s):  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Bovine Brain ◽  
Native Enzyme ◽  
Hydroxyl Groups ◽  
Inositol 1 ◽  
Substrate Structure ◽  
Purification And Properties ◽  
Phosphorylated Compounds ◽  
Hydrolysis Of

myo-Inositol-1-phosphatase from bovine brain was purified over 2000-fold. The native enzyme has a Mr of 59,000, and on SDS/polyacrylamide-gel electrophoresis the subunit Mr was 31,000. Thus the native enzyme is a dimer of two apparently identical subunits. The enzyme, purified to a specific activity of more than 300 units/mg of protein (1 unit of enzyme activity corresponds to the release of 1 mumol of Pi/h at 37 degrees C), catalysed the hydrolysis of a variety of phosphorylated compounds, the best one, in terms of V/Km, being D-myo-inositol 1-phosphate. Kinetic constants of compounds tested, including both isomers of glycerophosphate and two deoxy forms of beta-glycerophosphate, were measured. They show the importance of the two hydroxyl groups which are adjacent to the phosphate in myo-inositol 1-phosphate. With a wide variety of substrates Li+ was found to be an uncompetitive inhibitor whose Ki varied with substrate structure.

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