Characterization and partial purification of dl-glycerol-1-phosphatase from Dunaliella salina 

 -  Biochimica et Biophysica Acta, 661(2), p.199-204, 1981 .
<br/><br/> A specific DL-glycerol-l-phosphatase (glycerol-l-phosphate phosphohydrolase, EC 3.1.3.21)has been identified in the halotolerant alga Duniella salina. The enzyme is highly specific for DL-glycerol 1-phosphate, requires magnesium for activity and has a neutral pH optimum. High sensitivity toward sulfhydryl reagents suggests the existence of a sulfhydryl group in close proximity to the active site. Due to instability the enzyme was only partially purified (40-fold). Activity measurements following polyacrylamide electrophoresis showed the enzyme to have a molecular weight around 86 kdaltons. It is suggested that the enzyme plays a major role in the mechanism of osmoregulation in Dunaliella. 
<br/><br/><label>Subjects--Topical Terms: </label><br/>DL-GLYCEROL-L-PHOSPHATASE<br/>OSMOREGULATION<br/>GLYCEROL METABOLISM<br/>(DUNALIELLA SALINA)