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

Tipo de material: TextoTextoSeries ; Biochimica et Biophysica Acta, 661(2), p.199-204, 1981Trabajos contenidos:
  • Sussman, I
  • Avron, M
Tema(s): Recursos en línea: Resumen: 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.
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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.

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