Lipolytic enzymes in bovine thyroid tissue. II. Hydrolysis of [3H, 14C] phosphatidylethanolamine by neutral and alkaline phospholipase A activities.
Phospholipase and lysophospholipase activities are present in bovine thyroid (De Wolf et al., 1976). However, using exogenous [14C] phosphatidylcholine as substrate and subcellular fractions as enzyme source no activity could be detected at neutral and alkaline pH. Phospholipase A2 activity was found at neutral pH when [14C] phosphatidylethanolamine was substituted for [14C] phosphatidylcholine (De Wolf et al., 1976). In the present paper the occurrence of neutral and alkaline phospholipase A activities is clearly established. In addition their subcellular localization was investigated.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D004492:Edetic Acid / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010714:Phosphatidylethanolamines / Q000378:metabolism*; D010740:Phospholipases / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology; D013696:Temperature; D013961:Thyroid Gland / Q000201:enzymology*
D010714:Phosphatidylethanolamines; D004492:Edetic Acid; D010740:Phospholipases; D002118:Calcium