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090 _aB-12655
245 1 0 _aCharacterization and partial purification of dl-glycerol-1-phosphatase from Dunaliella salina
490 0 _vBiochimica et Biophysica Acta, 661(2), p.199-204, 1981
520 3 _aA 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.
650 1 4 _aDL-GLYCEROL-L-PHOSPHATASE
650 1 4 _aOSMOREGULATION
650 1 4 _aGLYCEROL METABOLISM
650 1 4 _a(DUNALIELLA SALINA)
700 1 2 _aSussman, I.
700 1 2 _aAvron, M.
856 4 0 _uhttps://drive.google.com/file/d/1PgnZ2bQZ1hIjFMs8T_3ZB2LzFOmfcsTl/view?usp=drivesdk
_zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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